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Porcine aminopeptidase

A recent study, however, has shown that aminopeptidase activity is present on the surface of porcine buccal mucosa, and that various aminopeptidase inhibitors, including amastatin and sodium deoxycholate, reduce the mucosal surface degradation of the aminopeptidase substrate, leucine-enkephalin [149], Since the peptidases are present on the surface of the buccal mucosa, they may act as a significant barrier to the permeability of compounds which are substrates for the enzyme. In addition to proteolytic enzymes, there exist some esterases, oxidases, and reductases originating from buccal epithelial cells, as well as phosphatases and carbohydrases present in saliva [154], all of which may potentially be involved in the metabolism of topically applied compounds. [Pg.94]

Two other very interesting applications of proteases are firstly the use of a protease to convert porcine insulin into human insulin, and secondly the use of L-aminopeptidase to produce the pharmaceutically useful substance p-phenylglycine by selectively hydrolyzing L-phenylglycinamide in a racemic mixture. [Pg.70]

Porcine kidney leucine aminopeptidase also binds one Zn2+ per subunit, which is essential for catalysis. The activity of the enzyme is regulated by the binding of divalent metal ions at a second site. [Pg.606]

In related work, Dong and Martin developed an assay that detects the catalytic activity of the enzymes pig liver esterase and porcine kidney leucine aminopeptidase by using substrates which have been labeled with metal-binding ligands [57], The enzymes catalyze changes in the substrates that affect their ability to bind to non-luminescent Ru complexes to form mixed-ligand complexes capable of ECL. [Pg.411]

Although the Edman method is by far the most common method of sequencing peptides from the /V-terminus, some enzymic methods are used occasionally. Several aminopeptidases are available commercially, which differ in their specificities. One aminopeptidase from porcine kidney preferentially releases amino acids such as leucine with hydrophobic side-chains. This enzyme does not release /V-terminal Arg or Lys or any amino acid that is followed by Pro. Another enzyme, aminopeptidase M, which is obtained from the microsomal fraction of porcine kidney cells, is less specific and perhaps more useful. It is advisable to examine aliquots of the hydrolysate at intervals by chromatography to determine the order in which amino acids are being released. [Pg.105]

Leucine aminopeptidase Porcine kidney 300,000 6 N-terminal exopeptidase Zn binds at two sites, one for catalysis, the other for regulation. [Pg.898]

The storage of porcine muscle homogenate at various pHs and 4 C for 5 days also shows that the increase in free amino acids is very small in an acidic pH region, while it is large under neutral pH (Figure 2). Since carboxypeptidase activities have been reported to be very slight in the muscle (55), the increase in free amino acids appears to be caused by the action of aminopeptidases which possess the optimal pH in the neutral region. [Pg.425]

Fig. 9.1. Linear relationship between molecular weight logarithm of globular proteins and log n (number of antigenic determinants) (from Louvard et ai, 1976). Abbreviations are as follows RNase pancreatic ribonuclease OV, ovalbumin BSA, bovine serum albumin yG, human IgG immunoglobulin PH, E. coli alkalin phosphatase Cat, liver catalase AP, porcine intestinal aminopeptidase. The following equations apply s = k s — /c2U, log M =... Fig. 9.1. Linear relationship between molecular weight logarithm of globular proteins and log n (number of antigenic determinants) (from Louvard et ai, 1976). Abbreviations are as follows RNase pancreatic ribonuclease OV, ovalbumin BSA, bovine serum albumin yG, human IgG immunoglobulin PH, E. coli alkalin phosphatase Cat, liver catalase AP, porcine intestinal aminopeptidase. The following equations apply s = k s — /c2U, log M =...

See other pages where Porcine aminopeptidase is mentioned: [Pg.11]    [Pg.11]    [Pg.336]    [Pg.429]    [Pg.151]    [Pg.94]    [Pg.177]    [Pg.77]    [Pg.738]    [Pg.342]    [Pg.428]   
See also in sourсe #XX -- [ Pg.11 ]




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