ISOLATION AND CHARACTERISTICS OF SCALLOP SARCOPLASMIC-RETICULUM WITH CALCIUM-TRANSPORT ACTIVITY

被引:7
作者
ABE, M
SHIRAKATA, Y
SATO, D
KONISHI, K
WATANABE, T
NAKAMURA, J
机构
[1] TOHOKU UNIV,FAC SCI,INST BIOL,AOBA KU,SENDAI,MIYAGI 980,JAPAN
[2] TOHOKU GAKUIN UNIV,FAC LIBERAL ARTS,SENDAI,MIYAGI 98131,JAPAN
[3] TOHOKU UNIV,COLL GEN EDUC,DEPT BIOL SCI,SENDAI,MIYAGI 980,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123983
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Sarcoplasmic reticulum with calcium transport activity has been isolated from the cross-striated adductor muscle of the scallop, which lives in cold (less-than-or-equal-to 20-degrees-C) sea water, by using pH 7.0 buffer solution both to homogenize the tissue and to sediment the membrane fraction. The yield of the preparation was 60-100 mg protein from 100 g of the scallop muscle. Ca2+-activated ATPase protein of about 100 kDa accounted for 40-50% of the protein preparation. The maximum activities of ATP-dependent, oxalate-facilitated calcium accumulation and Ca2+-ATPase were observed at a pH of about 7.0 and temperature of 20-30-degrees-C, and their values were about 2 mumol Ca2+/mg of protein/min and about 3 mumol ATP hydrolysis/mg of protein/min, respectively. At 0-degrees-C, 10-20% of these activities was maintained, while at 37-degrees-C, the activities were irreversibly lost. The Ca2+-ATPase activity was half-maximally activated at about 0.3 muM [Ca2+]. The ATPase activity exhibited non-Michaelian behavior with respect to ATP, with two different K(m) values of approximately 10 muM and 0.1-0.3 mM. GTP, CTP, and ITP were also hydrolyzed by the preparation at a rate of 10-30% of that of ATP. The preparation was stored at -80-degrees-C with retention of function for about a year.
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页码:822 / 827
页数:6
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