We have compiled a list of Best Reference Books on General Veterinary Biochemistry Subject. These books are used by students of top. Textbook of Veterinary Biochemistry: Medicine & Health Science Books @ by Larry R. Engelking August Bridging the gap between basic and clinical science concepts, the Textbook of Veterinary Physiological Biochemistry.

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Find Veterinary clinical biochemistry books online. Get the best Veterinary clinical biochemistry books at our marketplace. Textbook of Veterinary Biochemistry: Contents * Introduction * Physical Biochemistry * Carbohydrates * Lipids * Proteins * Amino Acids. Title, Textbook of Veterinary Biochemistry. Author, RS Dhanotiya. Edition, 2, revised. Publisher, Jaypee Brothers,Medical Publishers Pvt. Limited,

Longer stretches merit the title proteins. As an example, the important blood serum protein albumin contains amino acid residues.

A schematic of hemoglobin. The red and blue ribbons represent the protein globin ; the green structures are the heme groups. For instance, movements of the proteins actin and myosin ultimately are responsible for the contraction of skeletal muscle. One property many proteins have is that they specifically bind to a certain molecule or class of molecules—they may be extremely selective in what they bind.

Antibodies are an example of proteins that attach to one specific type of molecule.

Antibodies are composed of heavy and light chains. Two heavy chains would be linked to two light chains through disulfide linkages between their amino acids. Antibodies are specific through variation based on differences in the N-terminal domain.

Probably the most important proteins, however, are the enzymes.


Virtually every reaction in a living cell requires an enzyme to lower the activation energy of the reaction. These molecules recognize specific reactant molecules called substrates ; they then catalyze the reaction between them.

By lowering the activation energy , the enzyme speeds up that reaction by a rate of or more; a reaction that would normally take over 3, years to complete spontaneously might take less than a second with an enzyme.

The enzyme itself is not used up in the process, and is free to catalyze the same reaction with a new set of substrates. Using various modifiers, the activity of the enzyme can be regulated, enabling control of the biochemistry of the cell as a whole.

The primary structure of a protein consists of its linear sequence of amino acids; for instance, "alanine-glycine-tryptophan-serine-glutamate-asparagine-glycine-lysine-…". Secondary structure is concerned with local morphology morphology being the study of structure.

Clinical Biochemistry of Domestic Animals

Tertiary structure is the entire three-dimensional shape of the protein. This shape is determined by the sequence of amino acids.

In fact, a single change can change the entire structure. The alpha chain of hemoglobin contains amino acid residues; substitution of the glutamate residue at position 6 with a valine residue changes the behavior of hemoglobin so much that it results in sickle-cell disease.

Finally, quaternary structure is concerned with the structure of a protein with multiple peptide subunits, like hemoglobin with its four subunits. Not all proteins have more than one subunit. They can then be joined to make new proteins. Intermediate products of glycolysis, the citric acid cycle, and the pentose phosphate pathway can be used to make all twenty amino acids, and most bacteria and plants possess all the necessary enzymes to synthesize them.

Humans and other mammals, however, can synthesize only half of them. They cannot synthesize isoleucine , leucine , lysine , methionine , phenylalanine , threonine , tryptophan , and valine. These are the essential amino acids , since it is essential to ingest them. Mammals do possess the enzymes to synthesize alanine , asparagine , aspartate , cysteine , glutamate , glutamine , glycine , proline , serine , and tyrosine , the nonessential amino acids.

While they can synthesize arginine and histidine , they cannot produce it in sufficient amounts for young, growing animals, and so these are often considered essential amino acids.

The amino acids may then be linked together to make a protein. Total protein level increases due to dehydration, chronic inflammation, and paraproteinemia.

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It decreases due to overhydration, severe congestive heart failure with edema , protein-losing nephropathy, protein-losing enteropathy, hemorrhage, burns, dietary protein deficiency, malabsorption, and some viral conditions especially in horses.

Albumin level increases due to dehydration.

It decreases due to the same factors as total protein, plus liver failure. Urea level increases due to excess dietary protein, poor quality dietary protein, carbohydrate deficiency, catabolic states, dehydration, congestive heart failure, renal failure, blocked urethra, and ruptured bladder.

It decreases due to low dietary protein, gross sepsis, anabolic hormonal effects, liver failure, portosystemic shunts congenital or acquired , and inborn errors of urea cycle metabolism. Urea measurement is used especially to indicate renal disease and to a lesser extent liver dysfunction.

Creatinine level increases due to renal dysfunction, blocked urethra, and ruptured bladder. It decreases due to sample deterioration. Animals with a high muscle mass have high-normal creatinine concentrations, whereas animals with a low muscle mass have low-normal creatinine concentrations.

Creatinine measurement is used especially for renal disease. ALT is present in the cytoplasm and mitochondria of liver cells and, therefore, increases due to hepatocellular damage.

It has a half life of 2—4 hr and rises higher than AST but recovers quicker. There are minor increases with muscle damage and hyperthyroidism.

ALP level increases due to increased bone deposition, liver damage, hyperthyroidism, biliary tract disease, intestinal damage, hyperadrenocorticism, corticosteroid administration, barbiturate administration, and generalized tissue damage including neoplasia. The most common causes for an increase is raised levels of circulating steroids and biliary disease.

The half-life is 72 hr in dogs but only 6 hr in cats. Levels in the cat are generally much lower than in the dog, and any increase in cats is considered significant. In dogs, ALP levels in the thousands of units are usually associated with increased steroid levels. Slight level increases are reported in hypothyroidism. Only a very small amount of muscle damage such as bruising or IM injections can result in high serum CK levels. In dogs and cats, unless investigating specific muscle disease, increased levels are generally of no clinical significance.

Gershwin , Clinical Immunology.

Harvey , The Erythrocyte: Physiology, Metabolism, and Biochemical Disorders. Kaneko , Porphyrins and the Porhyrias. Smith , Iron Metabolism and Its Disorders. Dodds , Hemostasis. Zinkl and M. Kabbur , Neutrophil Function. Kramer and W.

Hoffmann , Clinical Enzymology. Tennant , Hepatic Function. Brobst , Pancreatic Function. Hornbuckle and B. Tennant , Gastrointestinal Function.

Finco , Kidney Function. Mol and A. Rijnberk , Pituitary Function. Rijnberk and J. Mol , Adrenocortical Function.

Kaneko , Thyroid Function. Edqvist and M. Forsberg , Clinical Reproductive Endocrinology. Rucker and J.

Morris , The Vitamins. Haskins and U.Write a product review. Gershwin , Clinical Immunology. Two of the most common polysaccharides are cellulose and glycogen , both consisting of repeating glucose monomers. VetBooks February 22, Harvey, Michael L. Information is provided on sampling techniques, the selection and use of an external laboratory, as well as near-patient testing and the practice laboratory.