Results 241 to 250 of about 2,710,839 (274)
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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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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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Calmodulin-binding proteins in smooth muscle
Archives Internationales de Physiologie et de Biochimie, 1984AbstractCalmodulin binding to its target proteins in smooth muscle microsomes was studied by means of [125I] calmodulin binding to nitrocellulose electroblots.
F. Wuytack +3 more
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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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Plant Molecular Biology, 2003
Ca2+ and calmodulin (CaM), a key Ca2+ sensor in all eukaryotes, have been implicated in defense responses in plants. To elucidate the role of Ca2+ and CaM in defense signaling, we used 35S-labeled CaM to screen expression libraries prepared from tissues that were either treated with an elicitor derived from Phytophthora megasperma or infected with ...
Vaka S, Reddy, Gul S, Ali, A S N, Reddy
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Ca2+ and calmodulin (CaM), a key Ca2+ sensor in all eukaryotes, have been implicated in defense responses in plants. To elucidate the role of Ca2+ and CaM in defense signaling, we used 35S-labeled CaM to screen expression libraries prepared from tissues that were either treated with an elicitor derived from Phytophthora megasperma or infected with ...
Vaka S, Reddy, Gul S, Ali, A S N, Reddy
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Trk is a calmodulin‐binding protein: implications for receptor processing
Journal of Neurochemistry, 2003AbstractThe tyrosine kinase receptors for the neurotrophins (Trk) are a family of transmembrane receptors that regulate the differentiation and survival of different neuronal populations. Neurotrophin binding to Trk leads to the activation of several signalling pathways including a rapid, but moderate, increase in intracellular calcium levels.
Marta, Llovera +7 more
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Extracellular calmodulin-binding proteins in body fluids of animals
Journal of Endocrinology, 1997Abstract The extracellular calmodulin-binding proteins (CaMBPs) were investigated in body fluids of animals by using the biotinylated calmodulin gel overlay method. Four major CaMBPs with molecular masses of 24, 31.5, 44/45 and 94 kDa were detected in serum, two of 24 and 63 kDa in bovine milk and three of 14, 24 and 52 kDa in human ...
T, WenQiang +4 more
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Identification of calmodulin-binding proteins.
Methods in enzymology, 1990We have outlined and partially characterized a series of biotinylated calmodulin derivatives that may be useful in the study of calmodulin-binding protein expression, physical points of calmodulin-target interaction, and proteolytic mapping of related calmodulin-binding proteins.
M L, Billingsley +3 more
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Expression of calmodulin and calmodulin binding proteins in lymphoblastoid cells
Journal of Cellular Physiology, 1994AbstractCalmodulin is encoded in vertebrates by three different genes: CALM1, CALM2, and CALM3. We have examined the mRNAs expressed from these three genes in eight lines of human lymphoblastoid cells (Namalwa, Raji, Ramos, JY, Molt‐4, Jurkat, CEM, and HPB‐ALL).
J, Colomer, N, Agell, P, Engel, O, Bachs
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