olhon.info Laws Modern Blood Banking And Transfusion Medicine 6th Edition Pdf


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Buy Modern Blood Banking & Transfusion Practices (Modern Blood Banking and (Modern Blood Banking and Transfusion Practice) 6th Edition, Kindle Edition. by . Immunology & Serology in Laboratory Medicine - E-Book (IMMUNOLOGY by the way has "B" in front of L! Third, it reads like a pdf!?!? and is very glitchy. 6th ed. p. ; cm. Modern blood banking and transfusion practices. Rev. ed. of: Modern blood banking entists and to apply it to everyday work in the blood bank. Download as PDF, TXT or read online from Scribd . 6th ed. p. ; cm. Modern blood banking and transfusion practices. Rev. ed. of: ough guide to transfusion practices and immunohematology. focuses on blood groups and routine blood bank.

Modern Blood Banking And Transfusion Medicine 6th Edition Pdf

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modern,blood,banking,transfusion,practices,harmening Thoroughly revised and updated, the 6th Edition of this popular text continues to set the standard for developing a Request an eBook to review for your course. Testing; Overview of the Routine Blood Bank Laboratory; Other Technologies and Automation. Modern blood banking and transfusion practices / [edited by] Denise M. resource] / [edited by] Denise Harmening. - 6th ed. Philadelphia: F.A. Davis, 1 online. Shop our inventory for Modern Blood Banking & Transfusion Practices - 6th Edition by Harmening, Denise M. Harmening with fast free shipping on every used.

The mechanism is thought to be due to disseminated intravascular coagulation, along with dilution of recipient platelets and coagulation factors. Close monitoring and transfusions with platelets and plasma is indicated when necessary. Metabolic alkalosis can occur with massive blood transfusions because of the breakdown of citrate stored in blood into bicarbonate. Hypocalcemia can also occur with massive blood transfusions because of the complex of citrate with serum calcium.

Blood doping is often used by athletes, drug addicts or military personnel for reasons such as to increase physical stamina, to fake a drug detection test or simply to remain active and alert during the duty-times respectively.

However a lack of knowledge and insufficient experience can turn a blood transfusion into a sudden death. For example, when individuals run the frozen blood sample directly in their veins this cold blood rapidly reaches the heart, where it disturbs the heart's original pace leading to cardiac arrest and sudden death.

Frequency of use[ edit ] Globally around 85 million units of red blood cells are transfused in a given year. The rate of hospitalizations with a blood transfusion nearly doubled from , from a rate of 40 stays to 95 stays per 10, population. It was the most common procedure performed for patients 45 years of age and older in , and among the top five most common for patients between the ages of 1 and 44 years. However, successive attempts by physicians to transfuse animal blood into humans gave variable, often fatal, results.

Pope Innocent VIII is sometimes said to have been given "the world's first blood transfusion" by his Jewish physician Giacomo di San Genesio, who had him drink by mouth the blood of three year-old boys.

The boys subsequently died. The evidence for this story, however, is unreliable and may have been motivated by anti-semitism. Working at the Royal Society in the s, the physician Richard Lower began examining the effects of changes in blood volume on circulatory function and developed methods for cross-circulatory study in animals, obviating clotting by closed arteriovenous connections.

The new instruments he was able to devise enabled him to perform the first reliably documented successful transfusion of blood in front of his distinguished colleagues from the Royal Society. According to Lower's account, " Then, to make up for the great loss of this dog by the blood of a second, I introduced blood from the cervical artery of a fairly large mastiff, which had been fastened alongside the first, until this latter animal showed … it was overfilled … by the inflowing blood.

Lower had performed the first blood transfusion between animals. He was then "requested by the Honorable [Robert] Boyle … to acquaint the Royal Society with the procedure for the whole experiment", which he did in December in the Society's Philosophical Transactions. Both instances were likely due to the small amount of blood that was actually transfused into these people.

This allowed them to withstand the allergic reaction. Denys's third patient to undergo a blood transfusion was Swedish Baron Gustaf Bonde.

He received two transfusions. Murphy M, Pamphilon D, editors. Boston: Blackwell Publishing; Web page with links to other documents on regulatory Bethesda: American information on blood-borne pathogens, needle-stick pre- Association of Blood Banks; Management training Apheresis Web site. Accreditation of Cellular Therapy Web site. Teaching pediatric laboratory medicine to We thank Paul Mintz, MD, who was responsible for the creation of pathology residents.

Arch Pathol Lab Med ; this task force. Simon TL. Comprehensive curricular goals for teaching transfusion medicine. Transfusion ; 1. Graylyn Conference Report. Recommendations for reform Conjoint Task Am J Clin Pathol ; Transfusion Medicine Academic Award Group. Curriculum content and evaluation of resident compe- Transfusion ; Hum Pathol Fellow- ; The role of physicians in blood centers.

Academy of Clinical Laboratory Physicians and Scientists. Transfusion ; Curriculum content and evaluation of resident compe- It was noted that incidence rates are approximately two times greater for first-time donors.

The use of nucleic acid amplification testing NAT under an Investigational New Drug Application since and now as tests licensed by the Food and Drug Adminis-tration FDA since is one reason for increased safety of the blood supply. Refer to Chapter 19 for a detailed discus-sion of transfusion-transmitted viruses. Normal chemical composition and structure of the RBC membrane 2.

Hemoglobin structure and function 3. RBC metabolism Defects in any or all of these areas will result in RBC survival of fewer than the normal days in circulation. Step 2: The Donor Health History Questionnaire A uniform donor history questionnaire designed to ask ques-tions that protect the health of both the donor and the recipient is given to every donor.

The health history questionnaire is used to identify donors who have been exposed to other diseases e. Step 3: The Abbreviated Physical Examination The abbreviated physical examination for donors includes blood pressure, pulse, and temperature readings, hemoglobin or hematocrit level, and the inspection of the arms for skin lesions. Lipids are not equally distributed in the two layers of the membrane.

The external layer is rich in glycolipids and choline phospholipids. In addition, they maintain a critical role in two important RBC character-istics: Deformability To remain viable, normal RBCs must also remain flexible, deformable, and permeable. The loss of adenosine triphos-phate ATP energy levels leads to a decrease in the phos-phorylation of spectrin and, in turn, a loss of membrane deformability.

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These cells are at a marked disadvantage when they pass through the small 3 to 5 m in diameter sinusoidal orifices of the spleen, an organ that functions in extravascular sequestration and removal of aged, damaged, or less deformable RBCs or fragments of their membrane.

The survival of these forms is also shortened. Any abnormality that increas-es permeability or alters cationic transport may lead to decrease in RBC survival. The RBC membrane is freely permeable to water and anions. Chloride Cl and bicarbonate HCO3 can traverse the membrane in less than a second. It is speculated that this massive exchange of ions occurs through a large number of exchange channels located in the RBC membrane.

RBC volume and water home-ostasis are maintained by controlling the intracellular concentrations of sodium and potassium. The erythrocyte intracellular-to-extracellular ratios for Na and K are 1: Numbers refer to pattern of migration of SDS sodium dodecyl sulfate poly-acrylamide gel pattern stained with Coomassie brilliant blue. Relations of protein to each other and to lipids are purely hypothetical; however, the posi-tions of the proteins relative to the inside or outside of the lipid bilayer are accurate.

Proteins are not drawn to scale and many minor proteins are omitted. Because the mature erythrocyte has no nucleus and there is no mitochondrial apparatus for oxida-tive metabolism, energy must be generated almost exclusive-ly through the breakdown of glucose. RBC metabolism may be divided among the anaerobic glycolytic pathway and three ancillary pathways that serve to maintain the structure and function of hemoglobin Fig.

All of these processes are essential if the erythro-cyte is to transport oxygen and to maintain critical physical characteristics for its survival. Approximately 10 percent is provided by the pentose phosphate pathway. The activity of this pathway increases fol-lowing increased oxidation of glutathione or decreased activ-ity of the glycolytic pathway. When the pentose phosphate pathway is functionally defi-cient, the amount of reduced glutathione becomes insuffi-cient to neutralize intracellular oxidants.

The result is denaturation and precipitation of globin as aggregates Heinz bodies within the cell. If membrane damage is sufficient, cell destruction occurs. The methemoglobin reductase pathway is another impor-tant pathway of RBC metabolism. Calmodulin, a cytoplas-mic calcium-binding protein, is speculated to control these pumps and to prevent excessive intracellular Ca2 buildup, which changes the shape and makes the RBC more rigid.

When RBCs are ATP-depleted, Ca2 and Na are allowed to accumulate intracellularly, and K and water are lost, result-ing in a dehydrated rigid cell subsequently sequestered by the spleen, resulting in a decrease in RBC survival.

In the absence of the enzyme methemoglo-bin reductase and the action of nicotinamide adenine dinu-cleotide NAD , there is an accumulation of methemoglobin, which results from a conversion of ferrous iron to the ferric form Fe3. Methemoglobin represents a nonfunctional form of hemoglobin and a loss of oxygen transport capabilities, inasmuch as metheme cannot bind with oxygen.

To illustrate the efficiency of this system, normal healthy individuals have no more than 1 percent methemoglobin circulating in their RBCs.

A defect in the methemoglobin reductase pathway is, therefore, significant to RBC posttransfusion survival and function. Hemoglobin Structure and Function Hemoglobin makes up approximately 95 percent of the dry weight of an RBC or approximately 33 percent of its weight by volume.

Normal hemoglobin consists of globin a tetramer of two pairs of polypeptide chains and four heme groups, each of which contains a protoporphyrin ring plus iron Fe2. Hemoglobin Synthesis Normal hemoglobin production is dependent on three processes: Adequate iron delivery and supply 2. Adequate synthesis of protoporphyrins the precursor of heme 3.

Adequate globin synthesis All adult normal hemoglobins are formed as tetramers con-sisting of two alpha chains plus two non- globin chains.

Normal adult RBCs contain the following types of hemoglo-bin: Each synthesized globin chain links with heme ferroproto-porphyrin IX to form hemoglobin, which normally consists of two chains, two chains, and four heme groups. The rate of globin synthesis is directly related to the rate of porphyrin synthesis and vice versa: The unloading of oxygen by hemoglobin is accompanied by widening of a space between chains and the binding of 2,3-DPG on a mole-for-mole basis, with the formation of anionic salt bridges between the chains.

The resulting conformation of the deoxyhemoglobin molecule is known as the tense T form, which has a lower affinity for oxygen. When hemoglo-bin loads oxygen and becomes oxyhemoglobin, the estab-lished salt bridges are broken, and chains are pulled together, expelling 2,3-DPG. This is the relaxed R form of the hemoglobin molecule, which has a higher affinity for oxy-gen.

These allosteric changes that occur as the hemoglobin loads and unloads oxygen are referred to as the respiratory movement. The dissociation and binding of oxygen by hemo-globin are not directly proportional to the partial pressure of oxygen PO2 in its environment but, instead, exhibit a sig-moid- curve relationship, known as the hemoglobin-oxygen dissociation curve Fig.

The shape of this curve is very important physiologically because it permits a considerable amount of oxygen to be delivered to the tissues with a small drop in oxygen tension.

For example, in the environment of the lungs, where the oxygen PO2 tension, measured in mil-limeters of mercury mm Hg , is nearly mm Hg, the hemoglobin molecule is almost percent saturated with oxygen. As the RBCs travel to the tissues, where the PO2 drops to an average 40 mm Hg mean venous oxygen tension , the hemoglobin saturation drops to approximately 75 percent sat-uration, releasing approximately 25 percent of the oxygen to the tissues.

This is the normal situation of oxygen delivery at basal metabolic rate. The normal position of the oxygen dissocia-tion curve depends on three different ligands normally found within the RBC: H ions, CO2, and organic phosphates. Of these three ligands, 2,3-DPG plays the most important physi-ologic role. Note in Figure 1—6 that the oxygen saturation of hemoglo-bin in the environment of the tissues 40 mm Hg PO2 is now 50 percent; the other 50 percent of the oxygen is being released to the tissues.

The RBCs thus have become more effi-cient in terms of oxygen delivery. Therefore, a patient who is suffering from an anemia caused by loss of RBCs may be able to compensate by shifting the oxygen dissociation curve to the right, making the RBCs, although few in number, more efficient.

Some patients may be able to tolerate anemia better than others because of this compensatory mechanism. A shift to the right may also occur in response to acidosis or a rise in body temperature.

The shift to the right of the hemoglobin-oxygen dissociation curve is only one way in which patients may compensate for various types of hypoxia. Other ways include an increase in total car-diac output and an increase in the production of RBCs eryth-ropoiesis.

With such a dissociation curve, RBCs are much less efficient because only 12 percent of the oxygen can be released to the tissues. Among the conditions that can shift the oxygen dissociation curve to the left are alkalosis; increased quantities of abnormal hemoglobins, such as methemoglobin and carboxyhemoglobin; increased quantities of hemoglobin F; and multiple transfusions of 2,3- DPG—depleted stored blood attesting to the importance of 2,3-DPG in oxygen release.

Hemoglobin-oxygen affinity can also be expressed by P50 values, which designate the PO2 at which hemoglobin is 50 percent saturated with oxygen under standard in-vitro conditions of temperature and pH. The P50 of normal blood is 26 to 30 mm Hg. An increase in P50 represents a decrease in hemoglobin-oxygen affinity, or a shift to the right of the oxy-gen dissociation curve.

A decrease in P50 represents an increase in hemoglobin-oxygen affinity, or a shift to the left of the oxygen dissociation curve. Abnormalities in hemoglobin structure or function can there-fore have profound effects on the ability of the RBCs to pro-vide oxygen to the tissues.

RBC Preservation The goal of blood preservation is to provide viable and func-tional blood components for patients requiring blood transfu-sion.

Because blood must be stored from the time of donation until the time of transfusion, the viability of RBCs must be maintained during the storage time as well. Seventy-five percent of cells that have been transfused should remain viable for 24 hours.

The measurements are made with RBCs that are taken from healthy subjects, stored and then labeled with radioisotopes, reinfused to the original donor, and measured 24 hours after transfusion.

To maintain optimum viability, blood is stored in the liq-uid state between 1 and 6C for a specific number of days, as determined by preservative solution s used.

These changes include a decrease in pH, a decrease in glucose con-sumption, a buildup of lactic acid, a decrease in ATP levels, and a reversible loss of RBC function. Because low 2,3-DPG levels profoundly influence the oxygen dissociation curve of hemoglobin,14 DPG-depleted RBCs may have an impaired capacity to deliver oxygen to the tissues. As RBCs in whole blood or RBC concentrates are stored, 2,3-DPG levels decrease, with a shift to the left of the hemoglobin-oxygen dissociation curve, and therefore less oxygen is delivered to the tissues.

It is well accepted, how-ever, that 2,3-DPG is re-formed in stored RBCs, after in-vivo circulation resulting in restored oxygen delivery. The rate of restoration of 2,3-DPG is influenced by the acid-base status of the recipient, phosphorus metabolism, and the degree of anemia. Therefore, a substitute preservative, CPD, came into widespread use in the United States in the s because it was superior for preserving this organic phosphate.

Modern Blood Banking & Transfusion Practices

This effect is the result of a higher pH Table 1—4. Subsequent studies led to the addition of various chemicals, along with the currently approved anticoagulant-preservative CPD, in an attempt to stimulate glycolysis so that ATP levels were better maintained. CPDA-1 contains 0. Adenine-supplemented blood can be stored at 1 to 6C for 35 days. The extra glucose was added because of the lengthened storage period. The reported pathophysiologic effects of the transfusion of RBCs with low 2,3-DPG levels and increased affinity for oxy-gen include an increase in cardiac output, a decrease in mixed venous PO2 tension, or a combination of these.

The physio-logic importance of these effects is not easily demonstrated. This is a complex mechanism with numerous variables involved that are beyond the scope of this text. Stored RBCs do regain the ability to synthesize 2,3-DPG after transfusion, but levels necessary for optimal hemoglobin oxygen delivery are not reached immediately.

Approximately 24 hours are required to restore normal levels of 2,3-DPG after transfusion. However, evidence suggests that, in the transfused subject whose capacity is lim-ited by an underlying physiologic disturbance, even a brief period of altered oxygen hemoglobin affinity is of great signif-icance. Several animal studies demonstrate significantly increased mortality associated with transfusing blood that is low in 2,3-DPG lev-els in subjects with persistent anemia, hypotension, hypoxia, and cardiac and hemorrhagic shock.

Human studies demon-strate that myocardial function improves following transfu-sion of blood with high 2,3-DPG levels during cardiovascular surgery.

It is apparent that many factors may limit the viability of transfused RBCs. One of these factors is the plastic material used for the storage container. The plastic must be sufficient-ly permeable to CO2 in order to maintain higher pH levels during storage. Glass storage containers are a matter of his-tory in the United States. Currently, all blood is stored in polyvinyl chloride PVC plastic bags Fig. One issue associated with PVC bags relates to the plasticizer, di ethyl-hexyl - phthalate DEHP , which is used in the manufacture of the bags.

It has been found to leach into the blood from the plastic into the lipids of the plasma medium and RBC mem-branes during storage. For mL collections, 70 mL of anticoagulant-preservative solution is used. Research has been focused on the development of improved plastic blood bags as well as better preservative solutions. In addition to blood preservation issues, adverse effects and risks associated with blood transfusion have created concern and caution among clinicians when determining the need for blood and blood components see Chapter Additive solutions are now widely used.

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One of the reasons for their development related to the fact that removal of the plas-ma component during the preparation of RBC concentrates removed much of the nutrients needed to maintain RBCs dur-ing storage.

This was dramatically observed when high hema-tocrit RBCs were prepared. The influence of removing substantial amounts of adenine and glucose present original-ly in, for example, the CPDA-1 anticoagulant-preservative solution led to a decrease in viability, particularly in the last 2 weeks of storage.

Additive solu-tions mL to the RBC concentrate prepared from a mL blood collection also overcome this problem. Additive solutions reduce hematocrits from around 70 to 85 percent to around 50 to 60 percent. The ability to pack RBCs to fairly high hematocrits before addition of additive solution also pro-vides a means to harvest greater amounts of plasma with or without platelets.

The configuration of the additive solution approach remains essentially unchanged. In general, the additive solutions employed in the systems were composed of standard ingredients used intravenously: Lovric dou-bled the dextrose concentration in the primary anticoagulant CP2D and used it in connection with an additive solu-tion composed of saline, adenine, glucose, trisodium citrate, citric acid, and sodium phosphate.

AS-1 Baxter Healthcare 2. It is coupled with CPD as the primary bag anticoagulant-preserva-tive. AS-3 contains SAG as in AS-1 but at different concen-trations and in addition to sodium phosphate, sodium citrate, and citric acid. It is coupled with CP2D as the primary bag anticoagulant-preservative.

All of these additive solutions are approved for 42 days of storage of RBCs.

Table 1—5 lists the currently approved additive solutions, and Table 1—6 describes formu-lations for each one. The formulations listed in Table 1—6 are for mL of additive solution that is added to RBCs prepared from mL blood collections.

When the collection systems are for mL of blood, the volume of the additive solution is mL. Overall, data from clinical studies show that RBCs stored for 42 days in AS-1, AS-3, or AS-5 demonstrated a mean hour postinfusion survival of greater than 75 per-cent, the minimum requirement for satisfactory RBC sur-vival.

Table 1—7 shows the biochemical characteristics of RBCs stored in the three additive solutions after 42 days of stor-age. Blood stored in additive solu-tions is now routinely given to newborn infants and pediatric patients,25 although some clinicians have continued to prefer CPDA-1 RBCs because of their concerns about one or more of the constituents in the additive solutions. None of the additive solutions maintain 2,3-DPG through-out the storage time.


Autologous transfusion allows individuals to donate blood for their own autologous use in meeting their needs for blood transfusion see Chapter The procedure for freezing a unit of packed RBCs is not complicated.

Basically, it involves the addition of a cryopro-tective agent to RBCs that are less than 6 days old.

Glycerol is used most commonly and is added to the RBCs slowly with vigorous shaking, thereby enabling the glycerol to permeate the RBCs. The cells are then rapidly frozen and stored in a freezer. The usual storage temperature is below 65C, although storage and freezing temperature depends on the concentration of glycerol used.

Table 1—8 lists the advantages of the high-concentration glycerol technique in comparison with the low-concentration glycerol technique. The reader is referred to Chapter 11 for a detailed description of the RBC freezing procedure. Transfusion of frozen cells must be preceded by a deglyc-erolization process; otherwise the thawed cells would be accompanied by hypertonic glycerol when infused, and RBC lysis would result.

Removal of glycerol is achieved by system-atically replacing the cryoprotectant with decreasing concen-trations of saline. The usual protocol involves washing with 12 percent saline, followed by 1. Excessive hemolysis is monitored by noting the hemoglo-bin concentration of the wash supernatant.

Osmolality of the unit should also be monitored to ensure adequate deglyc-erolization. Traditionally, because a unit of blood is processed under open system conditions to add the glycerol before freezing or the saline solutions for deglycerolization , the outdating period of thawed RBCs stored at 1 to 6C has been 24 hours.

Red blood cells stored in additive solutions such as AS-1 and AS-3 have been frozen up to 42 days after liquid storage without rejuvenation. Recently, an instrument ACP , Haemonetics has been developed that allows the glyc-erolization and deglycerolization processes to be performed under closed system conditions.

Based on approval by the FDA, RBCs prepared from mL collections and frozen within 6 days of blood collection with CPDA-1 can be stored after thawing at 1 to 6C for up to 15 days when the processing is conducted with the ACP instrument and the deglycerolized cells, prepared using salt solutions as in the traditional procedures, are suspended in the AS-3 additive solution as a final step, which is thought to provide stabiliza-tion to the thawed RBCs.

These storage conditions are based on the parameters used in a study by Valeri and others that showed that RBC properties were satisfactorily maintained during a day period. Currently, the FDA licenses frozen RBCs for a period of 10 years from the date of freezing; that is, frozen RBCs may be stored up to 10 years before thawing and transfusion.

Need to control freezing rate No Yes 3. Type of freezer Mechanical Liquid nitrogen 4. Shipping requirements Dry ice Liquid nitrogen 6. Effect of changes in storage temperature Can be thawed and refrozen Critical those of fresh blood.

Experience has shown that year storage periods do not adversely affect viability and func-tion. The initial rejuvenation solution contained phosphate, ino-sine, glucose, pyruvate, and adenine PIGPA.Transfusion-Transmitted Malaria in the United States from through Original comprehensive step by step illustrations of ABO forward and reverse grouping, not found in any other book, help the student to quickly master this important testing, which represents the foundation of blood banking.

The influence of removing substantial amounts of adenine and glucose present original-ly in, for example, the CPDA-1 anticoagulant-preservative solution led to a decrease in viability, particularly in the last 2 weeks of storage.

The normal platelet count ranges from , to , per L. Start on. Perioperative Roseff S, editor. The patient was consulted for a more complete medical history and reported that she had never traveled outside of the country. Likewise, histocompatibility testing also interfaces residency training. The presence of stromal elements in earlier unmodified formulations caused a variety of toxicological reactions, based primarily on animal testing.