Results 201 to 210 of about 77,245 (243)
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Calmodulin-binding protein of erythrocyte cytoskeleton
Biochemical and Biophysical Research Communications, 1981Abstract Previously we have shown that purified spectrin binds calmodulin in the presence of Ca2+ with a Kd value of 3 μM (Sobue, K. et al. (1980) Biochemistry International 1, 561–566). We now provide evidence that the calmodulin-binding activity found in the human erythrocyte cytoskeleton is indeed due to spectrin and no other binding proteins are ...
K, Sobue +3 more
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CALMODULIN-BINDING PROTEINS IN BRAIN
Neurochemistry International, 1983It is now widely accepted that actions of intracellular Ca(2+) are mediated by a four-domain Ca(2+)-binding protein, calmodulin. Brain is especially rich in calmodulin, containing about 400 mg (24 ?mol) of EGTA-extractable calmodulin per kg of brain. However, only a fraction of the above amount is required for the calmodulin-activated enzymes and most ...
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Calmodulin-binding protein kinases in plants
Trends in Plant Science, 2003Many calmodulin-binding protein kinases have been isolated from plants. Plant calmodulin-binding protein kinases are novel protein kinases that differ from calcium-dependent protein kinases in many important respects. Calmodulin-binding protein kinases are likely to be crucial mediators of responses to diverse endogenous and environmental cues in ...
Lei, Zhang, Ying-Tang, Lu
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Ca2+/calmodulin-binding proteins in Dictyostelium discoideum
Research in Microbiology, 1991We have initiated a systematic study of Ca2+/calmodulin-regulated enzymes in the cellular slime mold Dictyostelium discoideum. Using 125I-labelled D. discoideum calmodulin (CaM) as a functional probe, several Ca2+/CaM-binding proteins were detected in crude cell lysates.
T, Winckler, H, Dammann, R, Mutzel
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CALMODULIN AND CALMODULIN-BINDING PROTEINS IN PLANTS
Annual Review of Plant Physiology and Plant Molecular Biology, 1998▪ Abstract Calmodulin is a small Ca2+-binding protein that acts to transduce second messenger signals into a wide array of cellular responses. Plant calmodulins share many structural and functional features with their homologs from animals and yeast, but the expression of multiple protein isoforms appears to be a distinctive feature of higher plants ...
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Calmodulin binding proteins in rat liver mitochondria
Biochemical and Biophysical Research Communications, 1984Calmodulin binding proteins have been found in submitochondrial fractions obtained from highly purified rat liver mitochondria. The matrix fraction contains two major calmodulin binding proteins: one, having Mr of 145,000, apparently is carbamoyl-phosphate synthetase. Another has a Mr of 58,000 and has not been associated with enzyme activities.
P, Gazzotti, M, Gloor, E, Carafoli
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Calmodulin-binding proteins of Tetrahymena microsomal membranes
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985Tetrahymena calmodulin radioiodinated with a lactoperoxidase method retained full ability to activate Tetrahymena guanylate cyclase. Binding of [125I]calmodulin to Tetrahymena microsomal membranes was Ca2+-dependent and inhibited by excess unlabeled calmodulin or trifluoperazine.
S, Nagao, Y, Nozawa
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Caldesmon: A calmodulin — Binding actin — Regulatory protein
Cell Calcium, 1986The protein caldesmon, originally isolated from smooth muscle tissue where it is the most abundant calmodulin-binding protein, has since been shown to have a wide distribution in actin- and myosin- containing cells where it is localized in sub-cellular structures concerned with motility, shape changes and exo- or endo-cytosis.
K, Pritchard, C J, Moody
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Calmodulin Binding Proteins In Platelet Actomypsin
Thrombosis and Haemostasis, 1981Platelet actomyosin (thrombosthenin) possesses a myosin-linked Ca2+ regulation and Ca2+ sensitivity is conferred to it by calmodulin through myosin light chain kinase. Calmodulin binding proteins if they are present in the actomyosin complex may have an important regulatory role in the contractile mechanism of platelet activation.
L Muszbek, J Harsfalvi
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Journal of Neurochemistry, 1985
Abstract: The presence of calmodulin‐binding sites on chromaffin granule membranes has been investigated. Saturable, high‐affinity 125I‐calmodulin‐binding sites (KD= 9.8 nM; Bmax= 25 pmol/mg protein) were observed in the presence of 10−4M free calcium. A second, nonsaturable, calmodulin‐binding activity could also be detected at 10−7M free calcium. No
M F, Bader, T, Hikita, J M, Trifaró
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Abstract: The presence of calmodulin‐binding sites on chromaffin granule membranes has been investigated. Saturable, high‐affinity 125I‐calmodulin‐binding sites (KD= 9.8 nM; Bmax= 25 pmol/mg protein) were observed in the presence of 10−4M free calcium. A second, nonsaturable, calmodulin‐binding activity could also be detected at 10−7M free calcium. No
M F, Bader, T, Hikita, J M, Trifaró
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