title: N-terminal domain of pepsin as a model for retroviral dimeric aspartyl protease.
abstract: Autolysis of porcine pepsin at pH 4 affords a derivative possessing intrinsic proteolytic activity. This derivative was isolated by alumina pseudo-affinity chromatography and gel-filtration and was found to result from the tight association of two identical molecules, 135 amino acids long, emerging from the N-terminal domain of pepsin. This finding emphasizes a similarity with the only aspartyl-proteases known to act as dimers, the retroviral proteases.
authors.affiliation: INSERM U 58, Montpellier, France.
authors.forename: M
authors.initials: M
authors.lastname: Bianchi
authors.forename: R A
authors.initials: RA
authors.lastname: Boigegrain
authors.forename: B
authors.initials: B
authors.lastname: Castro
authors.forename: M A
authors.initials: MA
authors.lastname: Coletti-Previero
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002846:Chromatography, Affinity; D010450:Endopeptidases / Q000378:metabolism*; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine
chemical_list: D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A