Journal ArticleDOI
The presence of γ-carboxyglutamic acid-containing protein in atheromatous aortae
TLDR
The level of the γ-carboxyglutamic acid containing protein in atherogenic diet fed rat aortae exceeds that found normally in bone or in tissues predisposed for physiological calcification.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1979-12-14. It has received 14 citations till now. The article focuses on the topics: Carboxyglutamic acid & Valine.read more
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Age-related changes in composition and mechanical properties of the tunica media of the upper thoracic human aorta.
TL;DR: It is proposed that the morphological changes and the stiffening observed in the aging aortic wall are not due to degradation of its elastin network but to variations in the supramolecular organization connective tissue components.
Journal ArticleDOI
Inflammation and bone resorption as independent factors of accelerated arterial wall thickening in patients with rheumatoid arthritis.
Mayumi Nagata-Sakurai,Masaaki Inaba,Hitoshi Goto,Yasuro Kumeda,Yutaka Furumitsu,Kentaro Inui,Hidenori Koyama,Masanori Emoto,Eiji Ishimura,Tetsuo Shoji,Yoshiki Nishizawa +10 more
TL;DR: Patients with RA have a higher rate of increase in thickening of the arterial wall, and inflammation and calcium mobilization are factors closely associated with the accelerated arterIAL wall changes.
Journal ArticleDOI
Gamma-carboxyglutamic acid
TL;DR: Gamma-carboxyglutamic acid is an amino acid with a dicarboxylic acid side chain, with unique metal binding properties, that has been discovered in blood coagulation proteins, plasma proteins of unknown function, and proteins from calcified tissue.
Journal ArticleDOI
Vitamin K dependent carboxylation of glutamate residues to gamma-carboxyglutamate in microsomes from spleen and testes: comparison with liver, lung, and kidney.
TL;DR: Protein carboxylation in microsomes from extrahepatic tissues was greatly stimulated by manganese ions and was dependent upon the addition of dithioerythritol, while Menaquinone-3 was much more active than vitamin K1 in driving carboxyglutamate.
Journal ArticleDOI
Post-translational carboxylation of preprothrombin
TL;DR: The determination of the sites of possible regulation in the formation of an active enzyme protein was only possible after the overall pathway of active enzyme synthesis had been established and the finding of carboxylation as the vitamin K dependent step in prothrombin ‘completion’ became untenable.
References
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Journal ArticleDOI
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
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Determination of the Tryptophan Content of Proteins by Ion Exchange Chromatography of Alkaline Hydrolysates
Tony E. Hugli,Stanford Moore +1 more
TL;DR: A study of the variables in techniques for alkaline hydrolysis of proteins and for chromatographic analysis of the products has led to a method for the accurate determination of tryptophan which is applicable to foods and has been tested on normal and opaque-2 maize meals and on wheat flours.
Journal ArticleDOI
Vitamin K-dependent formation of gamma-carboxyglutamic acid.
J Stenflo,J W Suttie +1 more
TL;DR: An attempt is made to evaluate the phytochemical properties of the fruit extract of citric acid and its application in the treatment of neurological disorders.
Journal ArticleDOI
Chemical studies on methionyl-tRNA synthetase from Escherichia coli
C.J. Bruton,Brian S. Hartley +1 more
TL;DR: A technique is described which enables the amino acid sequence of small peptides to be determined when only nanomole quantities are available, suggesting that the subunits are identical and that conversion of tetramer to dimer does not involve proteolysis.
Journal ArticleDOI
Primary structure of the vitamin K-dependent part of prothrombin.
Staffan Magnusson,Staffan Magnusson,Lars Sottrup-Jensen,Lars Sottrup-Jensen,Torben E. Petersen,Torben E. Petersen +5 more
TL;DR: The first clue to the identity of the structural modification was the isolation of the tryptic peptides Gly-Phe-Leu-Glx- Glx-Val-Arg-Lys from positions 410 and 411 in normal prothrombin, which carried two negative charges more at neutral pH than could be attributed to normal glutamic acid residues.