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 language | English (US) |
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Pages (from-to) | 502-508 |
Number of pages | 7 |
Journal | Canadian journal of biochemistry |
Volume | 53 |
Issue number | 5 |
DOIs | |
State | Published - May 1975 |
Externally published | Yes |
ASJC Scopus subject areas
- General Medicine