Composition of the myosin light chain kinase from chicken gizzard

Da̧browska, Renata; Aromatorio, Debra K.; Sherry, James M. F.; Hartshorne, David J.

doi:10.1016/0006-291x(77)91429-2

Cited by 194 publications

(65 citation statements)

References 18 publications

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“…In addition, although CDR and troponin C possess limited biological crossreactivity, they are different proteins (3). In contrast to troponin C, CDR is an abundant (1-20 gM) and ubiquitous intracellular protein that regulates a number of enzymatic functions, including phosphodiesterase activation (4) and actomyosin ATPase activity (5,6), and has been implicated in microfilament organization (7). The development of monospecific antibodies to CDR has allowed the study of its distribution and localization by indirect immunofluorescence (8,*).…”

mentioning

confidence: 99%

Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

Marcum¹,

Dedman²,

Brinkley³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

434

170

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The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+ dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with anti-

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mentioning

confidence: 99%

Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

Marcum¹,

Dedman²,

Brinkley³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

434

170

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“…Phosphorylation of light chain 2 is catalyzed by a Ca2+-dependent protein kinase, referred to as myosin light chain kinase. The kinase is activated by the complex of Ca2+ and the calcium-dependent regulator protein (calmodulin) (3,4). It was originally identified in skeletal muscle (5) and, later, also in cardiac and smooth muscles and in nonmuscular tissues (for a review, see ref.…”

mentioning

confidence: 99%

Purification of myosin light chain kinase from bovine cardiac muscle.

Wolf¹,

Hofmann²

1980

Proc. Natl. Acad. Sci. U.S.A.

102

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Myosin light chain kinase was purified > 100,000-fold to apparent homogeneity with a yield of 10% from bovine cardiac muscle. Sodium dodecyl sulfate gels of the purified kinase showed one stained band corresponding to a Mr of 94,000. The enzyme was activated > 10-fold in the presence of Ca2+ (apparent Ka = 0.6-1.2 microM) and calmodulin (apparent Ka = 3-5 nM). The purified enzyme had a specific activity of 20-30 mumol of phosphate transferred per min per mg from ATP to cardiac myosin light chain 2. One mole of phosphate was incorporated per 94,000 g of the kinase in the presence of Ca2+ and calmodulin or of cyclic AMP-dependent protein kinase or of both additions. In addition to myosin light chain kinase, a calmodulin-binding protein of unknown function was purified from bovine cardiac muscle. This protein had a Mr of 85,000, was composed of two dissimilar subunits (Mr of 61,000 and 15,000), and competed with myosin light chain kinase for calmodulin. The protein appears to be closely related to the calmodulin-binding protein I purified from brain.

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“…The occurrence of calmodulin as a subunit of an enzyme has also been reported in some animal enzymes such as myosin light chain kinase of smooth muscle (22), and skeletal muscle phosphorylase kinase (23,24). However, the lysine-sensitive…”

Section: Discussionmentioning

confidence: 82%

Subunit structure of lysine sensitive aspartate kinase from spinach leaves

Kochhar

Sane

1998

IUBMB Life

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SummaryThe lysine -sensitive isoenzyme of aspartate kinase was purified to homogeneity from spinach leaves and its subunit composition was studied. The purified preparation had an apparent molecular mass of 280,000 and separated into two subunits-a large subunit with molecular mass of 53000 and smaller subunit with molecular mass of 17,000 by urea treatment and SDS PAGE. The enzyme molecule has subunit composition of 4 large and 4 small subunits. The activity of the large subunit was stimulated more than two fold by the addition of small subunit and the stimulated activity was inhibited by EGTA. This inhibition could be reversed by Ca + +. Further characteristics of the smaller subunit such as heat stability, behavior on ion exchange chromatography, elctrophoretic mobility on polyacrylamide gels, amino acid composition and pattern, presence of trimethyl lysine, its ability to activate other calmodulin stimulated enzymes and its calmodulin-like nature in RIA tests suggested that this subunit is identical to calmodutin.

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Composition of the myosin light chain kinase from chicken gizzard

Cited by 194 publications

References 18 publications

Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

Control of microtubule assembly-disassembly by calcium-dependent regulator protein.

Purification of myosin light chain kinase from bovine cardiac muscle.

Subunit structure of lysine sensitive aspartate kinase from spinach leaves

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