FEBS Letters | |
Covalent and non‐covalent interaction of chymotrypsin with α2‐macroglobulin | |
Delain, Etienne1  Favaudon, Vincent2  Tourbez, Martine2  Pochon, François2  | |
[1] Laboratoire de Microscopie Cellulaire et Moléculaire, Institut Gustave Roussy, 94805 Villejuif, France;Unité 219 INSERM, Institut Curie-Biologie, Centre Universitaire, 91405 Orsay France | |
关键词: Chymotrypsin; α2-Macroglobulin; Covalent interaction; Non-covalent interaction; Electrophoresis; α2M; α2-macroglobuIin; FITC; fluorescein isothiocyanate; I-AEDns; N-(iodoacetylaminoethyl)-5-naphthylamine-1-sulfonate; Hepes; N-(2-hydroxyethyl)piperazine-N′-2-ethanesulfonate; | |
DOI : 10.1016/0014-5793(87)81251-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The pattern of covalent crosslinking between human α2-macroglobulin (α2M) and chymotrypsin has been investigated by chromatography and polyacrylamide gel electrophoresis in denaturing medium. Reaction with a single mol of chymotrypsin per mol α2M results in the formation of a 95% covalent 1:1 chymotrypsin-α2M complex and in the proteolytic cleavage of both 180 kDa monomers in one α2M subunit. Proteolytic cleavage in the other α2M subunit requires the presence of a second mol of chymotrypsin; part (20%) of the protease in the 2:1 chymotrypsin-α2M complex thus formed appears to be non-covalently bound to the α2M chains. Covalent binding is abolished when the reaction of α2M with the protease is carried out in the presence of hydroxylamine. A single mol of the protease is then able to cleave all four 180 kDa monomers in α2M.
【 授权许可】
Unknown
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