Leucine aminopeptidase in extracts of swine muscle

Joseph, R. L.; Sanders, William J.

doi:10.1042/bj1000827

Cited by 22 publications

(5 citation statements)

References 8 publications

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“…LAP is also found in human peripheral lymphocytes and polymorphonuclear leukocytes (Smith et al 1983;Kohno and Kanno 1985). LAP is present in porcine muscle but the activity is low compared with kidney (Joseph and Sanders 1966). Rabbit LAP is present in renal proximal tubules, but not in glomeruli (Yang et al 1993).…”

Section: Cytosolic Dipeptidasesmentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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The mercapturic acid pathway is a major route for the biotransformation of xenobiotic and endobiotic electrophilic compounds and their metabolites. Mercapturic acids (N-acetyl-L-cysteine S-conjugates) are formed by the sequential action of the glutathione transferases, c-glutamyltransferases, dipeptidases, and cysteine S-conjugate N-acetyltransferase to yield glutathione S-conjugates, L-cysteinylglycine S-conjugates, L-cysteine S-conjugates, and mercapturic acids; these metabolites constitute a "mercapturomic" profile. Aminoacylases catalyze the hydrolysis of mercapturic acids to form cysteine S-conjugates. Several renal transport systems facilitate the urinary elimination of mercapturic acids; urinary mercapturic acids may serve as biomarkers for exposure to chemicals. Although mercapturic acid formation and elimination is a detoxication reaction, L-cysteine S-conjugates may undergo bioactivation by cysteine Sconjugate b-lyase. Moreover, some L-cysteine S-conjugates, particularly L-cysteinyl-leukotrienes, exert significant pathophysiological effects. Finally, some enzymes of the mercapturic acid pathway are described as the so-called "moonlighting proteins," catalytic proteins that exert multiple biochemical or biophysical functions apart from catalysis.

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Section: Cytosolic Dipeptidasesmentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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“…We are interested in the role of aminopeptidases in muscle protein catabolism, but these enzymes have not been closely studied in muscle. Joseph & Sanders (1966) purified leucine aminopeptidase from pig muscle and showed its properties to be generally similar to those of the well-known leucine aminopeptidase from kidney. Bury & Pennington (1973) separated two arylamidases and leucine amino.…”

mentioning

confidence: 77%

Separation of rat muscle aminopeptidases

Parsons¹,

Pennington²

1976

Biochemical Journal

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By means of chromatography on DEAE-Sephadex, two arylamidases (hydrolysing L-arginine 2-naphthylamide) and three dipeptidyl peptidases (hydrolysing dipeptide 2-naphthylamides) were distinguished in extracts of rat muscle. However, the arylamidase from the larger peak also hydrolysed the dipeptide 2-naphthylamides. Glycyl-L-arginine amide, an alternative substrate for dipeptidyl peptidase I, was not hydrolysed by arylamidase. L-Leucine amide was hydrolysed by an enzyme, presumed to be leucine aminopeptidase, from a separate peak, but was also hydrolysed by arylamidase. Arylamidase, dipeptidyl peptidase III and most of the leucine aminopeptidase could be extracted from the muscle with a neutral salt solution, but dipeptidyl peptidase I was extracted only in the presence of Triton X-100; dipeptidyl peptidase II showed an intermediate extraction behaviour.

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“…I kidney (9). Much less work has been done with a similar, perhaps identical, enzyme present in human serum (10).…”

Section: -10smentioning

confidence: 99%

Characterization of the protease activity in the chemotactic factor inactivator.

Ward¹,

Ozols²

1976

J. Clin. Invest.

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A B S T R A C T The chemotactic factor inactivator (CFI) isolated from human serum contains a kininase activity that causes extensive hydrolysis of bradykinin. The highly chemotactic synthetic peptide Met-Leu-Phe was completely hydrolyzed by CFI preparations. The release of the constituent amino acids from this peptide coincided with a loss of its chemotactic activity. The Nformyl, but not the amide derivative, of the leukotactic peptide Met-Leu-Phe was resistant to the action of CFI, as evidenced by chemotactic and biochemical assays. Examination of the specificity of CFI proteolysis revealed that short polypeptide substrates are degraded sequentially from the amino terminus. Larger peptides are less extensively hydrolyzed, and the patterns of hydrolysis are more complex. Inactivation of the bacterial chemotactic factors by CFI was overcome by the addition of high concentrations of peptides which were substrates for CFI. CFI preparations readily hydrolyzed the peptide Arg-Phe-Ala. The constituent amino acids were conveniently identified by thin-layer chromatography method. This procedure afforded a rapid assay for measuring CFI activity in the whole human serum as well as in fractions throughout the purification steps. Moreover, CFI also hydrolyzed L-leucyl-,8-napthylamide at rates comparable to peptides. Thus, L-leucyl-,Pnapthylamide served as a useful substrate for estimating CFI activity in preparations at various stages of purification. This substrate was also useful in kinetic studies. The results from these studies indicate an aminopeptidase activity is the mechanism whereby CFI inhibits the activity of chemotactic substrates.

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Leucine aminopeptidase in extracts of swine muscle

Cited by 22 publications

References 8 publications

The mercapturic acid pathway

The mercapturic acid pathway

Separation of rat muscle aminopeptidases

Characterization of the protease activity in the chemotactic factor inactivator.

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