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Subcellular distribution of myosin (K + , EDTA)‐ATPase in bovine adrenal medulla
Author(s) -
Hesketh John E.,
Aunis Dominique,
Pescheloche Michel,
Mandel Paul
Publication year - 1977
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(77)80467-5
Subject(s) - physics , citation , philosophy , microbiology and biotechnology , computer science , library science , biology
The presence of myosin-like proteins has been reported in several nervous tissues (for review, see ref. [l] ). Such a protein from the adrenal medulla has recently been characterized [2,3]. Knowledge of the localization of these proteins is poor but is of potential interest since it would provide information basic to evaluation of hypotheses concerning the function of actomyosin-like proteins in neurosecretion [4], ion transport [5], axoplasmic transport [6] and neuronal growth [7] . Myosin from both muscle and non-muscle sources is thought to be unique in possessing an ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity which is exhibited in the presence of 0.6 M KC1 and 2 mM EDTA [8]. Purification of myosin from various non-muscle tissues including the adrenal medulla [2,3] is associated with an increase in the specific activity of this (K’, EDTA)-ATPase. In the present work, such ATPase activity has been used as a biochemical marker for myosin with which to follow its distribution in subcellular fractions. The work was carried out using bovine adrenal medulla, a system well proven as a model for neurosecretion [9] .