Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase.

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Abstract Text:

M Milos,J J Schaer,M Comte,J A Cox,

Flow microcalorimetric titrations of calmodulin with seminalplasmin at 25 degrees C revealed that the high affinity one-to-one complex in the presence of Ca2+ (Comte, M., Malnoe, A., and Cox, J. A. (1986) Biochem. J. 240, 567-573) is entirely enthalpy-driven (delta H0 = -50 kJ.mol-1; delta S0 = O J.K-1.mol-1; delta Cp0 = O J.K-1.mol-1) and is not influenced by the proton or Mg2+ concentration. The Sr2+- and Cd2+-promoted high affinity complexes are also exothermic for -49 and -45 kJ.mol-1, respectively. The observed low affinity interaction in the absence of divalent ions displays no enthalpy change. No enthalpy changes are observed when calmodulin and seminalplasmin are mixed in the presence of millimolar concentrations of Mg2+, Zn2+, or Mn2+. Enthalpy titrations of the 1:1 calmodulin-seminalplasmin complex with Ca2+ and of partly Ca2+-saturated calmodulin with seminalplasmin revealed that only the species calmodulin.Can greater than or equal to 2 is fully competent for high affinity interaction with seminalplasmin. Binding of the second Ca2+ is strongly enhanced (K2 greater than or equal to 5 X 10(7) M-1) as compared to that in free calmodulin (K2 = 2.6 X 10(5) M-1). This is essentially due to the concomitant strongly exothermic step of isomerization of the calmodulin-seminalplasmin complex from its low to its high affinity form. Binding of the remaining two Ca2+ to the high affinity seminalplasmin-calmodulin complex displays the same affinity constants and endothermic enthalpy change as in free calmodulin. A microcalorimetric study on the complex formation between Ca2+-saturated calmodulin and turkey gizzard myosin light chain kinase revealed that the interaction is strongly exothermic with an important overall gain of order (delta H0 = -85 kJ.mol-1; delta S0 = -122 J.K-1.mol-1) and occurs with significant proton uptake (0.44 H+ per mol at pH 7.5). The observed low affinity interaction (K = 2.2 X 10(5) M-1) in the absence of Ca2+ (Mamar-Bachi, A., and Cox, J. A. (1987) Cell Calcium 8, 473-482) displays neither a change in enthalpy nor in protonation.

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Publishing Authors By Initials

M Milos,JJ Schaer,M Comte,JA Cox,

For similar animals: chordata: vertebrates: birds: galliformes: turkeys research abstracts see: animals: chordata: vertebrates: birds: galliformes: turkeys research

PUBMED ID PMID:

MEDLINE DATE:

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 263

Page Numbers: 9218-22

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 5

MONTH: Jul

YEAR: 1988

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Keywords Mesh Terms:

KEYWORDS: Turkeys

MESH TERMS: metabolism

Chemical & Substance for Abstract: Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase. Information

Substance Name: Myosin-Light-Chain Kinase

Registry Number: EC 2.7.1.117

Grant and Affiliation Information for Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase.

AFFILIATION: Department of Physical Chemistry, University of Geneva, Switzerland.

Country: UNITED STATES

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase Related Publications

• Absence of metabotropic glutamate receptor-mediated plasticity in the neocortex of fragile X mice.
• Affinity purification of seminalplasmin and characterization of its interaction with calmodulin.
• Australian parasitological research: now and in 2000.
• CD4+ T cell-dependent reduction in hepatitis C virus-specific humoral immune responses after HIV infection.
• Cancer and the threat of death: the cognitive dynamics of death-thought suppression and its impact on behavioral health intentions.
• Chapter 7: Achievements and limitations of cervical cytology screening.
• Costs of alcohol and drug-involved crime.
• Determination of ciglitazone in dog plasma by reversed-phase high-performance liquid chromatography.
• Effects of adult aging and hearing loss on comprehension of rapid speech varying in syntactic complexity.
• European psychiatry: moving towards integration and harmony.
• Experimental apparatus for the study of photoabsorption processes of multiply charged ions by synchrotron radiation.
• Genetic studies of stuttering in a founder population.
• Hypertonic saline reverses stiffness in a Sprague-Dawley rat model of acute intestinal edema, leading to improved intestinal function.
• Immune effector mechanisms in parasitic infections.
• Measurement of intestinal edema using an impedance analyzer circuit.
• Metabotropic glutamate receptors differentially regulate GABAergic inhibition in thalamus.
• Microcalorimetric investigation of the interaction of calmodulin with seminalplasmin and myosin light chain kinase.
• Modulation of thalamic neuron excitability by orexins.
• News from the WPA Secretariat.
• Non-human primate fetal kidney transcriptome analysis indicates mammalian target of rapamycin (mTOR) is a central nutrient-responsive pathway.
• Only time can tell: unethical research and the passage of time.
• Organized unidirectional waves of ATP hydrolysis within a RecA filament.
• Prenatal methyl mercury exposure from fish consumption and child development: a review of evidence and perspectives from the Seychelles Child Development Study.
• Protection against cryptococcosis by using a murine gamma interferon-producing Cryptococcus neoformans strain.
• Role of the vitamin D receptor in hair follicle biology.
• Studies of pituitary-adrenal-testis interaction in sheep. II. The effects of repeated injections of adrenocorticotrophic hormone outside the breeding season.
• The 12th world congress of psychiatry.
• The 13th World Congress of Psychiatry, Cairo 2005: perspectives from the Secretariat.
• Use of retrovirus expression of interfering RNA to determine the contribution of activated k-ras and ras effector expression to human tumor cell growth.
• Using inhibitors of prenylation to block localization and transforming activity.