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Molecular diversity of erythrocyte calpastatin.

Authors: E, Takano; M, Ueda; S, Tsunekawa; T, Murakami; M, Maki; M, Hatanaka; T, Murachi;

Molecular diversity of erythrocyte calpastatin.

Abstract

According to the difference of molecular masses estimated by SDS-polyacrylamide gel electrophoresis, calpastatins are classified into two types, i.e. muscle type (110 kDa) and erythrocyte type (70 kDa). Muscle type calpastatin contains four internally repetitive sequences (Domains 1-4) and one nonhomologous sequence on the amino-terminal side (Domain L), whereas erythrocyte type lacks Domains L and 1. By immuno-blot analysis, chicken erythrocytes, nucleated cells, were found to contain muscle type calpastatin. In avian erythrocytes, diminution of the calpastatin molecule as in mammalian erythrocytes was not observed.

Related Organizations
Keywords

Molecular Weight, Erythrocytes, Liver, Calpain, Calcium-Binding Proteins, Animals, Tissue Distribution, Chickens

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Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
13
Average
Top 10%
Average
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