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Start Over Author "Spamer, C." Journal biochemical and biophysical research communications
4 results on '"Spamer, C."'

3. Zn2+ Binding to Cardiac Calsequestrin

Author

Baksh, S., Spamer, C., Oikawa, K., Mccubbin, W.D., Heilmann, C., Kay, C.M., and Michalak, M.

Abstract

Zn2+ binding to canine cardiac calsequestrin was investigated using the Zn2+ specific fluorescence dye salicylcarbohydrazone (SACH), 65Zn2+ overlay and Zn2+-IDA chromatography. Cardiac calsequestrin binds ~200 moles of Zn2+/mole of protein with the Kd=300 µM. Zn2+ binding to calsequestrin was further confirmed by 65Zn2+ overlay and Zn2+-dependent aggregation of the protein. However, calsequestrin did not bind to a Zn2+-IDA-agarose column, indicating that histidine residues may not be involved in Zn2+ binding to the protein. Circular dichroism revealed only minor Zn2+-dependent conformational changes in calsequestrin. We conclude that calsequestrin is a Ca2+- and Zn2+-binding protein and that Zn2+ may modulate the structure and function of the protein.Copyright 1995, 1999 Academic Press, Inc.

Published
1995
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4. The phosphoprotein intermediate of a Ca2+ transport ATPase in rat liver endoplasmic reticulum.

Author

Heilmann C, Spamer C, and Gerok W

Subjects
Adenosine Triphosphatases metabolism, Animals, Biological Transport, Active, Ca(2+) Mg(2+)-ATPase, Calcium metabolism, Calcium-Transporting ATPases isolation & purification, Kinetics, Male, Molecular Weight, Phosphoproteins isolation & purification, Rats, Rats, Inbred Strains, Calcium-Transporting ATPases metabolism, Endoplasmic Reticulum enzymology, Liver enzymology, Phosphoproteins metabolism
Abstract

Smooth endoplasmic reticulum vesicles from rat liver display an ATP-supported Ca2+ transport which is mediated by a (Ca2+ + Mg2+)-ATPase. During the catalytic cycle the terminal phosphate from ATP is incorporated to form an acid-precipitable reaction product(118 000-Mr in SDS-gel electrophoresis) with stability characteristics of an acylphosphate. Comparative studies with sarcoplasmic reticulum vesicles from fast-twitch skeletal muscle suggest that the 118 000-Mr phosphopeptide may be identified with the phosphorylated reaction intermediate of a Ca2+ transport ATPase in endoplasmic reticulum, similar to that in sarcoplasmic reticulum of muscle.

Published
1983
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