Ovostatin: a novel proteinase inhibitor from chicken egg white. I. Purification, physicochemical properties, and tissue distribution of ovostatin.
作者： H Nagase , E D Harris , J F Woessner , K Brew
DOI: 10.1016/S0021-9258(18)32203-8
关键词: Egg white 、 Polyacrylamide gel electrophoresis 、 Collagenase 、 Monospecific antibody 、 Centrifugation 、 Biochemistry 、 Thermolysin 、 Protein quaternary structure 、 Guanidine 、 Chromatography 、 Chemistry
摘要: A proteinase inhibitor which has strong anti-collagenase activity was found in chicken egg white. The (pI = 4.9) purified by poly(ethylene glycol) (5.5-10%) precipitation and chromatography on Ultrogel AcA 34, DEAE-cellulose, Sephacryl S-300. final product homogeneous 5% polyacrylamide gel electrophoresis. Stoichiometric inhibition observed with the rabbit synovial collagenase thermolysin (1:1 molar ratio thermolysin). ran sodium dodecyl sulfate-gel electrophoresis reduction as a single protein band of Mr 165,000. molecular weight native estimated to be 780,000 sedimentation equilibrium centrifugation. Centrifugation analysis 6 M guanidine hydrochloride reduced sample gave omega 380,000 195,000, respectively, where is weight-average determined ultra-centrifugation. results indicated that molecule tetramer identical subunits linked pairs disulfide bonds. Since quaternary structure were similar those alpha 2-macroglobulin (alpha 2M) plasma, 2M isolated compared inhibitor. not sensitive methylamine, whereas was. No immunocross-reactivity between 2M. NH2-terminal sequence white Lys-Glu-Pro-Glu-Pro-Gln-Tyr-Val-Leu-Met-Val-Pro-Ala. Ser-Thr-Val-Thr-Glu-Pro-Gln-Tyr-Met-Val-Leu-Leu-Pro-Phe. Considerable homology two sequences human Monospecific antibody raised against employed examine tissue distribution only oviduct white, but other tissues or serum chickens.
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