Distribution of dipeptidase activity between lysosomes and soluble fraction of rat liver.

S. L. Taylor, A. L. Tappel

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Dipeptidase activity toward Arg-Phe, Arg-Gly, and Trp-Leu exhibited bimodal distribution in the lysosomal and soluble fractions of rat liver. The majority (50-70 percent) of the dipeptidase activity was present in the soluble fraction. Some evidence for a plasma membrane dipeptidase, which hydrolyzes Trp-Leu but not Arg-Phe or Arg-Gly, also was found. The lysosomal dipeptidase activity had a pH optimum of 6.0-7.0, and was activated by sulfhydryl reagents. Lysosomal localization for some of the dipeptidase activity was established with Triton WR-1339 fractionation and latency experiments.

Original languageEnglish (US)
Pages (from-to)502-508
Number of pages7
JournalCanadian journal of biochemistry
Volume53
Issue number5
DOIs
StatePublished - May 1975

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Lysosomes
tryptophan-leucine
Liver
Sulfhydryl Reagents
Cell Membrane
dipeptidase

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Distribution of dipeptidase activity between lysosomes and soluble fraction of rat liver. / Taylor, S. L.; Tappel, A. L.

In: Canadian journal of biochemistry, Vol. 53, No. 5, 05.1975, p. 502-508.

Research output: Contribution to journalArticle

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