Studies on Rat Parotid-cell Actomyosin

Overview

Journal Biochem J

Specialty Biochemistry

Date 1984 May 15

PMID 6331411

Citations 1

Authors

T Kealey

P J Randle

Affiliations

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Abstract

Actomyosin was partially purified from rat parotid cells dispersed by collagenase digestion and found to possess different solubility characteristics from that from (undispersed) rat parotid tissue. This is attributed to the decrease in vascular contamination effected by the isolation of parotid cells, yielding a non-muscle actomyosin [Adelstein, Conti, Johnson, Pastan & Pollard (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 3693-3697]. Myosin light-chain kinase was partially purified from dispersed rat parotid cells by calmodulin affinity chromatography and shown to be activated by Ca2+-calmodulin. The calmodulin content of dispersed rat parotid cells was shown to be 6.50 +/- 0.59 ng of calmodulin/micrograms of rat parotid-cell protein (mean +/- S.E.M.), as determined by the activation of purified bovine brain phosphodiesterase by heat-treated extracts of dispersed rat parotid cells.

Citing Articles

Mechanism of action of extracellular calcium on isoprenaline-evoked amylase secretion from isolated rat parotid glands.

Argent B, Arkle S J Physiol. 1985; 369:337-53.

PMID: 2419548 PMC: 1192653. DOI: 10.1113/jphysiol.1985.sp015905.

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