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Radiation inactivation analysis of kidney microvillar peptidases
Author(s) -
Fulcher Ian S.,
Ingram Jean,
Kenny A.John
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80921-8
Subject(s) - enzyme , dimer , aminopeptidase , monomer , chemistry , biochemistry , kidney , membrane , dipeptidyl peptidase , biology , leucine , amino acid , organic chemistry , endocrinology , polymer
Five membrane peptidases were studied by radiation inactivation analysis of pig kidney microvillar membranes. One heterodimeric enzyme, γ‐glutamyl transferase, presented a target size corresponding to the dimeric M r . The other enzymes are known to be homodimers. Three of these, aminopeptidase A, aminopep‐tidase N and dipeptidyl peptidase IV, gave results clearly indicating the monomer to be the target and, hence, in this group the association of the subunits was not essential for activity. The target size for endopep‐tidase‐24.11 was intermediate between those for monomer and dimer and its functional state was not resolved by the experiments.