Peptide Hydrolases

Marks, Neville

doi:10.1007/978-1-4615-7160-5_5

Cited by 2 publications

(2 citation statements)

References 154 publications

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“…The resulting supernatant was used for the analysis of AP activities and proteins. In this fraction, the major enzyme activity was previously described (Marks, 1970). All preparative steps were carried out at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Cyclic Changes of Exopeptidase Activities in the Rat Brain: a Regional Study

Gandarias

Echevarrı́a²,

Irazusta³

et al. 2009

Exp Clin Endocrinol Diabetes

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The present report describes the activity of three neuropeptide-degrading enzymes, in 12 brain areas during the estrous cycle of Sprague-Dawley rats. The quantitation of the enzyme activities was performed by measuring the rate of hydrolysis of the chromogenic substrates Leu-, Lys- and Asp-2-naphthylamides, by neutral, basic and acid aminopeptidase (AP) activities, respectively. Lys- and Leu-AP activities show a significant increase during the proestrus stage in the hypothalamus and the pituitary gland. Also there is a significant increase of Leu-AP activity in the occipital cortex. No significant decreases for Asp-AP activity during the proestrus in the hypothalamus and the pituitary were observed. As the changes seem to be limited at the hypothalamic-pituitary axis, these findings could be interpreted to mean that these exopeptidase activities play a role in the hormonal changes that take place during the estrous cycle of the rat.

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Section: Methodsmentioning

confidence: 99%

Cyclic Changes of Exopeptidase Activities in the Rat Brain: a Regional Study

Gandarias

Echevarrı́a²,

Irazusta³

et al. 2009

Exp Clin Endocrinol Diabetes

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“…It may arise from extracellular spaces of heart tissue, having escaped, perhaps, from erythrocytes, which are known to contain an arginine aminopeptidase (Makinen & Makinen, 1971). Peak-II (and peak-I) enzymes may belong to a wider group of arylamidases termed 'arylamidase N' (Marks, 1970), since the nitroanilide derivative hydrolysed contains a neutral amino acid. Many arylamidases that hydrolyse these derivatives, however, also hydrolyse others, e.g.…”

Section: Dialysis Against Metal-ion Chelatorsmentioning

confidence: 99%

Separation and properties of two arylamidases from rat cardiac-muscle extracts

Bury¹,

Coolbear²,

Savery³

1977

Biochemical Journal

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Two main arylamidase activities were separated from a particle-free supernatant of rat heart by chromatography on DEAE-Sephadex. Although both enzymes hydrolysed L-leucine 4-nitroanilide, only peak-II enzyme hydrolysed L-lysine 4-nitroanilide. A third minor peak (Ia) contained an enzyme that was active mainly on the L-lysine 4-nitroanilide. The mol.wts. of the enzymes in peaks I and II were approx. 257000 and 105000 respectively. The pH optimum was approx. pH7.0 for peak-I enzyme and 7.0-8.0 for peak-II enzyme. Both enzymes were inhibited by addition of puromycin, p-hydroxymercuribenzoate, o-phenanthroline and bivalent metal ions. Addition of dithiothreitol resulted in stimulation of both activities. Dialysis against o-phenanthroline resulted in inhibition of peak-I and -II enzymes, but after dialysis against EDTA only peak-II enzyme was inhibited.

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Peptide Hydrolases

Cited by 2 publications

References 154 publications

Cyclic Changes of Exopeptidase Activities in the Rat Brain: a Regional Study

Cyclic Changes of Exopeptidase Activities in the Rat Brain: a Regional Study

Separation and properties of two arylamidases from rat cardiac-muscle extracts

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