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      Gastrointestinal Function

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          This chapter describes the normal biochemical processes of intestinal secretion, digestion, and absorption. The digestive system is composed of the gastrointestinal (GI) tract, or the alimentary canal, salivary glands, the liver, and the exocrine pancreas. The principal functions of the gastrointestinal tract are to digest and absorb ingested nutrients, and to excrete waste products of digestion. Most nutrients are ingested in a form that is either too complex for absorption or insoluble, and therefore, indigestible or incapable of being digested. Within the GI tract, much of these substances are solubilized and further degraded enzymatically to simple molecules, sufficiently small in size, and in a form that permits absorption across the mucosal epithelium. This chapter explains in detail the mechanisms of salivary secretions, compositions of saliva, and the functions of saliva. The chapter also elaborates properties of bile as well as the synthesis of bile acids. The chapter explores the pathogenesis of the important gastrointestinal diseases of domestic animals, and the biochemical basis for their diagnosis and treatment. The chapter concludes with a discussion on disturbances of gastrointestinal function such as vomition, acute diarrheas, malabsorption, bacterial overgrowth, and ulcerative colitis.

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          Glutathione and related gamma-glutamyl compounds: biosynthesis and utilization.

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            Role of proteolytic enzymes in biological regulation (a review).

            Many enzymes, hormones, and other physiologically active proteins are synthesized as inactive precursors (zymogens) that are subsequently converted to the active form by the selective enzymatic cleavage (limited proteolysis) of peptide bonds. The ultimate agency of activating enzymatic function is limited proteolysis, either in a single activation step or in a consecutive series (cascade). The specificity of each activation reaction is determined by the complementarity of the zymogen substrate and the active site of the attacking protease. The sequence of consecutive activation reactions is regulated by the specificity of each enzyme, whereas the degree of amplification of the initial stimulus is determined by the efficiency of each activating step. Zymogen activation produces a prompt and irreversible response to a physiological stimulus, and is capable of initiating new physiological functions. Typical examples are the precesses of blood coagulation, fibrinolysis, complement activation, hormone production, metamorphosis, fertilazation, supra-molecular assembly, and digestion. The zymogens of the pancreatic serine proteases, in particular, have served as models for detailed studies of the nature of the molecular changes that are involved in the dramatic increase in enzymatic activity that ensues upon limited proteolysis of the zymogen.
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              Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system.

              Treatment of pigeon erythrocyte membranes with cholera toxin and NAD(+) enhanced the GTP stimulation and suppressed the F(-) activation of the adenylate cylase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1]. In the presence of NAD(+) labeled with (32)P in the AMP moiety the toxin catalyzed the covalent incorporation of radioactivity into membrane proteins with molecular weights (M(r)s) of 200,000, 86,000, and 42,000. Extraction of toxin-treated membranes with Lubrol PX followed by affinity chromatography on a GTP-Sepharose column resulted in a 200-fold purification of the 42,000-M(r) labeled protein and in its complete separation from the other labeled proteins. The fraction containing the purified GTP-binding component from toxin-treated membranes conferred an enhanced GTP-stimulated activity on adenylate cyclase solubilized from nontreated membranes. Likewise, the addition of GTP-binding fraction from nontreated membranes to an enzyme solubilized from toxin-treated membranes restored F(-) stimulation of the adenylate cyclase. The toxin-induced modification of adenylate cyclase and the incorporation of radioactivity into the 42,000-M(r) protein were partially reversed upon incubation with toxin and nicotinamide at pH 6.1. The results indicate that cholera toxin affects the adenylate cyclase system by catalyzing an ADP-ribosylation of the 42,000-M(r) component bearing the guanyl nucleotide regulatory site.
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                Author and article information

                Journal
                Clinical Biochemistry of Domestic Animals
                Clinical Biochemistry of Domestic Animals
                22 October 2008
                2008
                22 October 2008
                : 413-457
                Affiliations
                [1 ]Department of Clinical Sciences, New York State College of Veterinary Medicine, Cornell University Ithaca, New York
                [2 ]Department of Clinical Sciences, New York State College of Veterinary Medicine, Cornell University Ithaca, New York
                [3 ]Department of Clinical Sciences, New York State College of Veterinary Medicine, Cornell University Ithaca, New York
                Article
                B978-0-12-370491-7.00014-3
                10.1016/B978-0-12-370491-7.00014-3
                7173558
                965ab4e9-43ea-4001-b26b-31395466d3b4
                Copyright © 2008 Elsevier Inc. All rights reserved.

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