Amino‐Acid Sequence of an α‐Parvalbumin, PI = 4.88, from Frog Skeletal Muscle
- 1 April 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 123 (2), 337-345
- https://doi.org/10.1111/j.1432-1033.1982.tb19773.x
Abstract
The primary structure of the most basic (pI [isoelectric point] = 4.88) of the 2 major parvalbumins from frog skeletal muscle (R. esculenta) was determined by partial automatic sequencing of the protein which exhibits a free N terminus, thermolysin and Armillaria mellea protease. This protein showed the typical structure of an .alpha.-parvalbumin. Comparison of the primary structure of ion-binding loops of .alpha.- and .beta.-parvalbumins did not provide a clear-cut explanation of their differences in ion-binding properties.Keywords
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