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Purification and characterization of the parvalbumin from monkey skeletal muscle

Authors
Journal
Comparative Biochemistry and Physiology Part B Comparative Biochemistry
0305-0491
Publisher
Elsevier
Publication Date
Volume
96
Issue
4
Identifiers
DOI: 10.1016/0305-0491(90)90211-b
Disciplines
  • Biology
  • Medicine

Abstract

Abstract 1. 1. A high affinity Ca 2+ binding and low mol. wt protein, parvalbumin, was purified from monkey skeletal muscle. 2. 2. As compared with other animals, only one component and a lower content of monkey parvalbumin were found. 3. 3. This may suggest that both the component and the content of parvalbumin decreases with biological evolution. 4. 4. The parvalbumin was found to have a mol. wt of 11,400, a pI of 5.1, a high aspartic acid and lysine content, maximum absorption at around 260nm, a blocked amino-terminal, an immunological distinction, 2 mol Ca 2+ binding/mol, and a conformational change by Ca 2+ binding. 5. 5. Parvalbumin was shown to have alpha type properties.

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