Effect of K+, and other ligands on the thiol reactivity and tryptic cleavage pattern of scallop sarcoplasmic reticulum

1989 ◽  
Vol 10 (3) ◽  
pp. 229-244 ◽  
Author(s):  
Peter M. D. Hardwicke ◽  
Piroska Huvos
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Cleavage Pattern ◽  
Tryptic Cleavage ◽  
Thiol Reactivity

Tryptic cleavage of sarcoplasmic reticulum protein

Biochemistry ◽  
1974 ◽  
Vol 13 (16) ◽  
pp. 3298-3306 ◽  
Author(s):  
Giuseppe Inesi ◽  
Donald Scales
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Tryptic Cleavage

scholarly journals Mouse α-macroglobulin. Structure, function and a molecular model

1987 ◽  
Vol 248 (3) ◽  
pp. 837-845 ◽  
Author(s):  
N W Hudson ◽  
J M Kehoe ◽  
P H Koo
Keyword(s):  
Structural Model ◽  
Peptide Mapping ◽  
Molecular Model ◽  
Binding Property ◽  
Cleavage Pattern ◽  
Terminal Sequence ◽  
Binding Studies ◽  
Tryptic Cleavage ◽  
Before And After ◽  
A Minor

Mouse alpha-macroglobulin (M-AMG) is believed to be a functional homologue of human alpha 2-macroglobulin (h-alpha 2M). The subunit composition, the tryptic cleavage pattern before and after methylamine incorporation and the two-dimensional tryptic-peptide mapping, however, indicate that these two proteins are structurally distinct. M-AMG is composed of two major types of polypeptides (Mr 163,000 and 35,000) together with a minor polypeptide (Mr 185,000), whereas h-alpha 2M has only one type of polypeptide (Mr 185,000). After incorporation of methylamine, there is no change in the normal tryptic-cleavage pattern of M-AMG; however, tryptic cleavage of h-alpha 2M is severely retarded [Hudson & Koo (1982) Biochim. Biophys. Acta 704, 290-303]. The N-terminal sequence of the 163,000-Mr polypeptide of M-AMG shows sequence homology with the N-terminal sequence of h-alpha 2M. The amino acid compositions of M-AMG and its two major polypeptide chains are compared. Thermal fragmentation studies show that the 163,000-Mr polypeptide is broken down into 125,000-Mr and 29,000-Mr fragments. Trypsin-binding studies show that M-AMG can bind two molecules of trypsin/molecule. Inactivations of the trypsin-binding property of M-AMG and h-alpha 2M with methylamine show similar kinetics of inhibition at 4 degrees C. A structural model of M-AMG is proposed, based on accumulated data.

scholarly journals Tryptic cleavage inhibits but does not uncouple Ca2+ATPase of sarcoplasmic reticulum

1988 ◽  
Vol 173 (2) ◽  
pp. 361-367 ◽  
Author(s):  
Katalin TOROK ◽  
Brian J. TRINNAMAN ◽  
N. Michael GREEN
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Tryptic Cleavage

scholarly journals The effect of actin and phosphorylation on the tryptic cleavage pattern of Acanthamoeba myosin IA

1989 ◽  
Vol 264 (17) ◽  
pp. 10243-10250
Author(s):  
H Brzeska ◽  
T J Lynch ◽  
E D Korn
Keyword(s):  
Cleavage Pattern ◽  
Tryptic Cleavage

Localization of E1–E2 conformational transitions of sarcoplasmic reticulum Ca-ATPase by tryptic cleavage and hydrophobic labeling

1986 ◽  
Vol 93 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Jens P. Andersen ◽  
Bente Vilsen ◽  
John H. Collins ◽  
Peter L. Jørgensen
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Conformational Transitions ◽  
Tryptic Cleavage

scholarly journals A Disulfide Bond at Cys 190 of Tropomyosin Alters Tryptic Cleavage Pattern

2010 ◽  
Vol 98 (3) ◽  
pp. 349a-350a
Author(s):  
John P. Sumida ◽  
David Yampolsky ◽  
Sherwin S. Lehrer
Keyword(s):  
Disulfide Bond ◽  
Cleavage Pattern ◽  
Tryptic Cleavage

A Reproducible Selective Stain for Cardiac Sarcoplasmic Reticulum

1974 ◽  
Vol 32 ◽  
pp. 214-215
Author(s):  
R. A. Waugh ◽  
J. R. Sommer
Keyword(s):  
Complex System ◽  
Electron Microscope ◽  
Sarcoplasmic Reticulum ◽  
Transmission Electron Microscope ◽  
Electron Microscopic ◽  
Cardiac Sarcoplasmic Reticulum ◽  
Transmission Electron

Cardiac sarcoplasmic reticulum (SR) is a complex system of intracellular tubules that, due to their small size and juxtaposition to such electron-dense structures as mitochondria and myofibrils, are often inconspicuous in conventionally prepared electron microscopic material. This study reports a method with which the SR is selectively “stained” which facilitates visualizationwith the transmission electron microscope.

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