Hog pancreas

ENZYMATIC ANALYSIS WITH CARBOXYPEPTIDASES. Carboxypeptidases are enzymes that cleave amino acid residues from the C-termini of polypeptides in a successive fashion. Four carboxypeptidases are in general use A, B, C, and Y. Carboxypeptidase A (from bovine pancreas) works well in hydrolyzing the C-terminal peptide bond of all residues except proline, arginine, and lysine. The analogous enzyme from hog pancreas, carboxypeptidase B, is effective only when Arg or Lys are the C-terminal residues. Thus, a mixture of carboxypeptidases A and B liberates any C-terminal amino acid except proline. Carboxypeptidase C from citrus leaves and carboxypeptidase Y from yeast act on any C-terminal residue. Because the nature of the amino acid residue at the end often determines the rate at which it is cleaved and because these enzymes remove residues successively, care must be taken in interpreting results. Carboxypeptidase Y cleavage has been adapted to an automated protocol analogous to that used in Edman sequenators. 

The answer is d. (Hardman, p 935.) Pancrelipase is an alcoholic extract of hog pancreas that contains lipase, trypsin, and amylase. It is effective in reducing the steatorrhea of pancreatic insufficiency None of the other drugs mentioned have significant action in the digestion of fats... 

The fiber fraction was washed several times with water, ratio 1 5, the washings being added to the starch fraction (Figure 2). Final traces of starch were removed from the fiber by incubation with 2% alpha-amylase (Sigma Chemical Co., type V-A from hog pancreas) for 16 hr at 37°C, and washing several times with distilled water before freeze-drying. 

G. candidum, R. arrhizus, R. delemar, hog pancreas and hog liver esterase (15). Especially R. arrhizus and R. delemar lipases were found capable of hydrolyzing various kinds of polyesters (Table I). 

Exocrine pancreatic insufficiency is most commonly caused by cystic fibrosis, chronic pancreatitis, or pancreatic resection. When secretion of pancreatic enzymes falls below 10% of normal, fat and protein digestion is impaired and can lead to steatorrhea, azotorrhea, vitamin malabsorption, and weight loss. Pancreatic enzyme supplements, which contain a mixture of amylase, lipase, and proteases, are the mainstay of treatment for pancreatic enzyme insufficiency. Two major types of preparations in use are pancreatin and pancrelipase. Pancreatin is an alcohol-derived extract of hog pancreas with relatively low concentrations of lipase and proteolytic enzymes, whereas pancrelipase is an enriched preparation. On a per-weight basis, pancrelipase has approximately 12 times the lipolytic activity and more than 4 times the proteolytic activity of pancreatin. Consequently, pancreatin is no longer in common clinical use. Only pancrelipase is discussed here. 

Hog pancreas lipase Succinic anhydride Diethyl ether, room temp, 48 h E 12... 

U a-amylase (hog pancreas a-amylase Sigma-Aldrich) Bring to 1 liter with distilled water Adjust to pH 7... 

Crystalline alpha-amylases have been prepared from hog pancreas, human pancreas and saliva, " rat pancreas, malted barley, Aspergillus oryzae, - - Pseudomonas saccharophila, Bacillus subtilis, °- Bacillus coagulans, and Bacillus stearothermoph-ilus, whilst extensively purified enzymes have been obtained from malted sorghum, soya beans,broad beans, malted wheat, pigeon pancreas, and shore crab. The preparative procedures usually involve precipitations by ammonium sulfate and acetone. 

The amino acid compositions of the alpha-amylase from human saliva, hog pancreas, Bacillus suhtilfs, B. stearothermo-philus, Aspergillus oryzae, and malted sorghum have been determined and are shown in Table III. The results show that alpha-amylases from these different sources differ widely in structure. In particular, it is to be noted that cystine and cysteine were not found in the alpha-amylase from B. subtilis. The sequence of amino acids or the three-dimensional structure of any one alpha-amylase is not yet known. The enzyme from A. oryzae differs from the others further, because it is a glycoprotein containing a small proportion of carbo-hydrate. ... 

Human saliva Hog pancreas Bacillus subtUis - Bacillus stearo-thermophilus Aspergillus oryzae - Malted sorghum ... 

Fig. 5.—The Smallest, Resistant Dextrins Obtained on the a-Amylolysis of Starch, Using Enzymes from (a) Hog Pancreas, Human Saliva, and Aspergillus oryzae (b) Malted Barley and (c) Bacillus subtilus." [Q. a-D-glucose residue , reducing D-glucose residue —a-D-(l— 4) bond , a-D-(l- 6) bond.]...

Transfer activity has been demonstrated in the hog pancreas alpha-amylase, but, again, the degree was extremely small. 

Comparison of Experimental and Theoretical Yields of Maltodextrins from Amylose by Action" of Hog-pancreas alpha-Amylase... 

Another common method for determination of alpha-samylase involves measurement of the diminution of the iodine-stainability of whole starch or amylopectin )8-limit dextrin. These methods are useful, as very small quantities of alpha-amylase may be estimated in this way. They are comparative, and cannot be used to determine rates of bond scission, unless they are carefully calibrated by a method that measures reducing end-groups. Such a calibration has been made for the action of hog-pancreas alpha-amylase on waxy-maize starch, although the validity of the reducing-power determinations, made with iodine and thiosulfate, has been confirmed for maltose only thus, it is not yet known whether the calibration is actually valid for the experimental system in which larger oligomers, for example, the triose and tetraose, are also formed. 

Estimations of and inhibition studies are, however, more valid, because determinations of absolute rates of bond scission are not necessary. The Michaelis constants for several alpha-amylases have been determined, and are shown in Table XI it may be seen that wide variations occur. For hog-pancreas alpha-amylase, it has been claimed that the value of depends on the degree of hydrolysis of the substrate this is probably true for all alpha-amylases when high degrees of hydrolysis are reached. 

The inhibition of aZp/ta-amylases from malt barley and hog pancreas by maltose has been shown to be noncompetitive, as has the inhibition of the malt-barley enzyme by a limit dextrin obtained by... 

Srivastava et al. [12] studied the esterification of myristic acid with ethanol with crude hog pancreas lipase. Conversions of up to 76% were obtained under solvent-free conditions while conversions of only up to 37% and 4% were obtained in scCO and acetonitrile, respectively. However, for similar enzyme concentrations, 37% of the myristic acid was converted to ester in scCO, but only 4% was converted in acetonitrile and solvent-free conditions. The alcohol was also found inhibitory for the reaction in scCO. ... 

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