Purification of calpain II from rat lens and determination of endogenous substrates.
作者： Larry L. David , Thomas R. Shearer
DOI: 10.1016/0014-4835(86)90057-6
关键词:
摘要: Abstract Calpain II ( EC 3.4.22.17), a calcium-dependent neutral protease, was purified approximately 7000-fold from the soluble fraction of rat lens. The estimated molecular weight lens calpain 120 000, and enzyme composed 80 000 28 MW subunits. required 400 μ m calcium, reducing agent, pH = 7·5 for maximal activity. could not be activated by magnesium, inhibited leupeptin iodoacetate, but phenylmethylsulfonyl fluoride. Purified degraded α-, β H -, L -crystallins, insoluble proteins, intrinsic membrane proteins. γ-Crystallin degraded. proteolysis caused similar to occurring during formation several experimental cataracts in rodents; this suggested that may play role cataract formation.
elsevier.com
sci-hub.se 参考文章(27)
L L David, T R Shearer, Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis. Investigative Ophthalmology & Visual Science. ,vol. 25, pp. 1275- 1283 ,(1984)
P Russell, In vitro alterations similar to posttranslational modification of lens proteins. Investigative Ophthalmology & Visual Science. ,vol. 25, pp. 209- 212 ,(1984)
John Kay, Ca2 - Activated Proteinases, Protein Degradation and Muscular Dystrophy Advances in Experimental Medicine and Biology. ,vol. 167, pp. 519- 531 ,(1984) , 10.1007/978-1-4615-9355-3_46
K R Hightower, S E Harrison, G Duncan, Intracellular calcium concentration and calcium transport in the rabbit lens. Investigative Ophthalmology & Visual Science. ,vol. 26, pp. 1032- 1034 ,(1985)
I Tsukahara, T Murachi, H Yoshida, Distribution of calpain I, calpain II, and calpastatin in bovine lens. Investigative Ophthalmology & Visual Science. ,vol. 26, pp. 953- 956 ,(1985)
Debdutta Roy, Raul Chiesa, Abraham Spector, Lens calcium activated proteinase: Degradation of vimentin Biochemical and Biophysical Research Communications. ,vol. 116, pp. 204- 209 ,(1983) , 10.1016/0006-291X(83)90401-1
L. J. Takemoto, J. S. Hansen, J. Horwitz, Comparison of in vitro proteolysis products of the normal human lens with putative in vivo proteolysis products of the cataractous lens Current Eye Research. ,vol. 2, pp. 849- 854 ,(1982) , 10.3109/02713688209020021
H YOSHIDA, T MURACHI, I TSUKAHARA, Limited proteolysis of bovine lens α-crystallin by calpain, A Ca2+-dependent cysteine proteinase, isolated from the same tissue Biochimica et Biophysica Acta. ,vol. 798, pp. 252- 259 ,(1984) , 10.1016/0304-4165(84)90313-1
Joram Piatigorsky, Peter F. Kador, Jin H. Kinoshita, Differential synthesis and degradation of protein in the hereditary Philly mouse cataract Experimental Eye Research. ,vol. 30, pp. 69- 78 ,(1980) , 10.1016/0014-4835(80)90125-6
Karen R. Fleshman, B.J. Wagner, Changes during aging in rat lens endopeptidase activity Experimental Eye Research. ,vol. 39, pp. 543- 551 ,(1984) , 10.1016/0014-4835(84)90054-X