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Distinctive catalytic actions of carp dipeptidases from ordinary muscle and intestine.

Journal of marine biotechnology

Aranishi F, Watanabe T, Osatomi K, Cao M, Hara K, Ishihara T.
PMID: 9701637
J Mar Biotechnol. 1998 Aug;6(3):157-62.

Although carp muscular and intestinal dipeptidases are metalloenzymes acting only on dipeptides, some structural and enzymatic differences occur between them. The present study verifies distinctive actions during dipeptide hydrolysis by these enzymes in terms of their kinetic characterization. The...

Cleavage of di- and tripeptides by Prevotella ruminicola.

Anaerobe

Wallace RJ, Kopecny J, Broderick GA, Walker ND, Sichao L, Newbold CJ, McKain N.
PMID: 16887545
Anaerobe. 1995 Dec;1(6):335-43. doi: 10.1006/anae.1995.1036.

The final step in the conversion of protein to amino acids by the common Gram-negative rumen bacterium, Prevotella (formerly Bacteroides) ruminicola , is the cleavage of di- and tripeptides. Dipeptidase and tripeptidase activities were predominantly cytoplasmic, and toluene treatment...

Mobilization of proline in the starchy endosperm of germinating barley grain.

Planta

Mikola L, Mikola J.
PMID: 24306246
Planta. 1980 Jul;149(2):149-54. doi: 10.1007/BF00380876.

In germinating grains of barley, Hordeum vulgare L. cv. Himalaya, free proline accumulated in the starchy endosperm during the period of rapid mobilization of reserve proteins. When starchy endosperms were separated from germinating grains and homogenized in a dilute...

Purification and partial characterization of a dipeptidase from barley.

Plant physiology

Sopanen T.
PMID: 16659587
Plant Physiol. 1976 Jun;57(6):867-71. doi: 10.1104/pp.57.6.867.

A peptidase hydrolyzing the dipeptide Ala-Gly optimally at pH 8 to 9 was purified about 3500-fold from germinated grains of barley (Hordeum vulgare L.). According to disc electrophoresis in the presence of sodium dodecyl sulfate, the preparation was about...

Showing 1 to 4 of 4 entries