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Fluorescence energy transfer between porcine pepsin and dansyl-peptide inhibitor

Journal Article · · Biophys. J.; (United States)
;
Activation of porcine pepsinogen by exposure to low pH leads to the release of the 44 amino terminal residues in the form of several peptide fragments. Peptide has been shown to be a strong inhibitor of the proteolytic activity of pepsin at pH 5.5, with K/sub 1/ of 0.2 ..mu..M. We have prepared several analogs of this sequence by solid phase peptide synthesis to examine the critical functional residues for this inhibition.
Research Organization:
Univ. of florida, Gainesville
OSTI ID:
6795768
Journal Information:
Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
Country of Publication:
United States
Language:
English

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Related Subjects

550200* -- Biochemistry
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ACID PROTEINASES
BIOCHEMICAL REACTION KINETICS
DYNAMIC FUNCTION STUDIES
ENERGY TRANSFER
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
FLUORESCENCE
HYDROLASES
KINETICS
LUMINESCENCE
ORGANIC COMPOUNDS
PEPSIN
PEPTIDE HYDROLASES
PEPTIDES
PROTEINS
REACTION KINETICS
STRUCTURAL CHEMICAL ANALYSIS