By F. John Gennari, Horacio J. Adrogue, John H. Galla, Nicolaos Maddias
With specific contributions and examine from specialists within the body structure of ordinary acid-base homeostasis and the administration of acid-base problems, this reference provides an abundance of knowledge on acid-base body structure, problems of acid-base equilibrium, and the administration and therapy of those problems in medical perform. a different and well timed resource, this advisor presents numerous tables, references, and figures to demonstrate the connection among the underlying body structure and analysis of acid-base problems.
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Extra resources for Acid-Base Disorders and Their Treatment
The pH at which there is no net charge is termed the isoelectric point and is unique for each protein. If the isoelectric point is at a pH lower (more acid) than the physiological level, then the protein exists in vivo as a polyanion. If the isoelectric point is more alkaline, then the protein is a polycation in vivo. The dominant proteins in plasma exist as polyanions, contributing to the anion gap (see Chapter 28) (36–38). 1 mmol=g=pH (17,36,37). From this value and normal protein concentration (70 g=L), one can calculate that their contribution to buffer0 Table 3 Intrinsic pK Values for Dissociable Groups of Various Body Proteins Dissociable groups (amino acid) a-carboxyl b-carboxyl (aspartic acid) g-carboxyl (glutamic acid) Imidazole (histidine) a-amino Sulfhydryl (cysteine) e-amino (lysine) Phenolic (tyrosine) Guanidino (arginine) Source: From Ref.
These isoforms also normally operate to cause a loss of alkali from cells. In some experimental models, the ClÀ=HCOÀ 3 exchanger appears to be activated by an increase in intracellular pH and to be inactivated by low cell pH, thus serving to regulate cell pH homeostatically in states of alkalemia (34). This property appears to occur primarily in cells of renal origin. Regulatory Control of Cell pH Cells contain a variety of membrane transporters that are candidates for regulatory Hþ extrusion. , the HþATPase) but most are dependent on the activity of cell membrane Naþ=Kþ ATPase to develop the necessary chemical and electrical gradients for linked Hþ extrusion or alkali entry.
19. Severinghaus JW, Stupfel M, Bradley AF. Accuracy of blood pH and PCO2 determinations. J Appl Physiol 1956; 9:189–196. 20. Maren TH. Carbonic anhydrase: chemistry, physiology, and inhibition. Physiol Rev 1967; 47:595–781. 21. Garg LC, Maren TH. The rates of hydration of carbon dioxide and dehydration of carbonic acid at 37 degrees. Biochim Biophys Acta 1972; 261:70–76. 22. Geers C, Gros G. Carbon dioxide transport and carbonic anhydrase in blood and muscle. Physiol Rev 2000; 80:681–715. 23. Gibbons BH, Edsall JT.
Acid-Base Disorders and Their Treatment by F. John Gennari, Horacio J. Adrogue, John H. Galla, Nicolaos Maddias