Crystalline structure of sarcoplasmic reticulum from scallop.
نویسندگان
چکیده
منابع مشابه
Crystalline structure of sarcoplasmic reticulum from scallop
Negatively stained sarcoplasmic reticulum from the scallop Placopecten magellanicus presented a variety of crystalline forms, the most common being tubular structures. These were characterized by paired rows of morphological units, spaced at approximately 120 A, running diagonally across the tubules. The orthogonal unit cell (120 X 55 A) contained two units, related by a twofold axis, which pro...
متن کاملVariation of scallop sarcoplasmic reticulum Ca2+-ATPase activity with temperature.
Methods for preparing native scallop sarcoplasmic reticulum vesicles, largely purified membranous scallop sarcoplasmic reticulum Ca2+-ATPase, and nonionic detergent-solubilized sarcoplasmic reticulum Ca2+-ATPase are described. The effect of a range of polyoxyethylene-based detergents on the solubilized Ca2+-ATPase was tested. Decaethylene glycol dodecyl ether (C12E10) supported the highest leve...
متن کاملEffect of Ca2+ on the dimeric structure of scallop sarcoplasmic reticulum
Scallop sarcoplasmic reticulum (SR), visualized in situ by freeze-fracture and deep-etching, is characterized by long tubes displaying crystalline arrays of Ca2+-ATPase dimer ribbons, resembling those observed in isolated SR vesicles. The orderly arrangement of the Ca2+-ATPase molecules is well preserved in muscle bundles permeabilized with saponin. Treatment with saponin, however, is not neede...
متن کاملSarcoplasmic Reticulum
Fragmented sarcoplasmic reticulum (FSR) membranes isolated from rabbit skeletal muscle are impermeable to inulin-(14)C (mol wt 5,000), and dextran-(14)C (mol wt 15,000-90,000) at pH 7.0-9.0, yielding an excluded space of 4-5 microl/mg microsomal protein. In the same pH range urea and sucrose readily penetrate the FSR membrane. EDTA or EGTA (1 mM) increased the permeability of microsomes to inul...
متن کاملEffect of orthophosphate, nucleotide analogues, ADP, and phosphorylation on the cytoplasmic domains of Ca(2+)-ATPase from scallop sarcoplasmic reticulum.
The effects of orthophosphate, nucleotide analogues, ADP, and covalent phosphorylation on the tryptic fragmentation patterns of the E1 and E2 forms of scallop Ca-ATPase were examined. Sites preferentially cleaved by trypsin in the E1 form of the Ca-ATPase were detected in the nucleotide (N) and phosphorylation (P) domains, as well as the actuator (A) domain. These sites were occluded in the E2 ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1983
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.97.2.557