-transparent.png){kind=logo}
Trypsin-like and carboxypeptidase B-like proteinases are believed to play important roles in the conversion of proinsulin into insulin as well as in the intracellular processing of a variety of other precursor forms. To facilitate the study of these enzymes we have developed sensitive methods for their detection in tissue preparations and incubation media. Studies with rat islet homogenates indicate the presence of both trypsin-like and carboxypeptidase B-like activities with slightly acidic pH optima. The trypsin-like activity was activated by thiols and inhibited by several thiol reagents but the carboxypeptidase was inhibited only by chelating agents. These properties suggest that these enzymes are related to the tissue cathepsins. Additional experimental approaches to the problems of positively identifying and localizing converting enzymes at the subcellular level are briefly discussed.
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
December 1988,
Neuroscience letters,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
February 1970,
Biochemical and biophysical research communications,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
October 1977,
Biochemical and biophysical research communications,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
April 1989,
Scandinavian journal of clinical and laboratory investigation,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
February 1973,
Endocrinology,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
April 1979,
The Biochemical journal,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
January 1984,
Biochimie,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
February 1974,
Diabetologia,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
December 1989,
The Biochemical journal,
H Zühlke, and
D F Steiner, and
A Lernmark, and
C Lipsey
April 2006,
Endocrine,
