Processing Endoprotease Recognizes a Structural Feature at the Cleavage Site of Peptide Prohormones
نویسندگان
چکیده
منابع مشابه
Signal peptidases recognize a structural feature at the cleavage site of secretory proteins.
The cloning of the gene for staphylococcal nuclease A in the pIN-III-OmpA secretion vector results in a hybrid protein which is processed by signal peptidase I, yielding an active form of the nuclease that is secreted across the cytoplasmic membrane (Takahara, M., Hibler, D., Barr, P. J., Gerlt, J. A., and Inouye, M. (1985) J. Biol. Chem. 260, 2670-2674). Using oligonucleotide-directed site-spe...
متن کاملProcessing-independent analysis of peptide hormones and prohormones in plasma.
Peptide hormones are post-translationally matured before they reach a structure in which they can fulfill their biological functions. The prohormone processing may encompass a variety of endoproteolytic cleavages, N- and C-terminal trimmings, and amino acid derivatizations. The same prohormone can be variably processed in different cell types and, in addition, diseased cells often change the pr...
متن کاملSite-selective chemical cleavage of peptide bonds.
Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid re...
متن کاملCleavage of honeybee prepromelittin by an endoprotease from rat liver microsomes: identification of intact signal peptide.
It has previously been shown that rat liver microsomes contain a proteolytic enzyme that cleaves honeybee prepromelittin to yield promelittin. This enzyme has now been further purified by centrifugation on a sucrose-deoxycholate gradient and then reconstituted into phospholipid vesicles. Incubation of prepromelittin with vesicles in the presence of melittin yields, in addition to promelittin, a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)71565-2