Key result
The complete primary structure of rat skeletal muscle peptidylarginine deiminase was deduced from isolated cDNA clones, revealing a 75,122 Da protein with a potential N-linked glycosylation site.
Population
Rat skeletal muscle and other tissues (spinal cord, cerebrum, cerebellum, submaxillary gland, liver, kidney)
Design
Preclinical
Authors
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No immediate clinical utility; extends PAD molecular characterization in rodents and leaves open human disease relevance.
The study determined the complete primary structure of rat skeletal muscle peptidylarginine deiminase and mapped its mRNA tissue distribution.
Watanabe et al. (1989) studied this question. cDNA cloning of rat skeletal muscle peptidylarginine deiminase was evaluated on Complete primary structure and mRNA expression. The complete primary structure of rat skeletal muscle peptidylarginine deiminase was deduced from isolated cDNA clones, revealing a 75,122 Da protein with a potential N-linked glycosylation site.
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