نتایج جستجو برای: Histidine

تعداد نتایج: 13716  

Journal: :European journal of pharmacology 2005
Yuan-ti Lee Cheng-chin Hsu Meng-hsiao Lin Keh-sen Liu Mei-chin Yin

In vivo effects of histidine and carnosine against diabetic deterioration in diabetic Balb/cA mice were studied. Histidine and carnosine at 0.5, 1 g/l were added into drinking water. After 4 weeks intake of these agents, the content of histidine and carnosine in plasma, heart and liver significantly elevated (P < 0.05). The intake of these agents significantly decreased plasma glucose and fibro...

2014
Marcos Aurélio Barboza de Oliveira Antônio Carlos Brandi Carlos Alberto dos Santos Paulo Henrique Husseni Botelho José Luís Lasso Cortez Moacir Fernandes de Godoy Domingo Marcolino Braile

INTRODUCTION Solutions that cause elective cardiac arrest are constantly evolving, but the ideal compound has not yet been found. The authors compare a new cardioplegic solution with histidine-tryptophan-glutamate (Group 2) and other one with histidine-tryptophan-cetoglutarate (Group 1) in a model of isolated rat heart. OBJECTIVE To quantify the fractal dimension and Shannon entropy in rat my...

Journal: :The Journal of biological chemistry 1971
B P Rosen F D Vasington

A histidine-binding protein has been isolated from the shock fluid of osmotically shocked Salmonella typhimurium cells and has been purified by conventional techniques. It has a molecular weight of 25,000 and binds 1 histidine molecule per molecule of protein. The binding protein is stable to wide variations of temperature, ionic strength, and pH. It binds histidine with a KD of 1.5 pM. The pro...

Journal: :The Biochemical journal 1963
V G ZANNONI B N LA DU

In studies on the nature of the enzymic defect in patients with histidinaemia, an inborn error of histidine metabolism (La Du, Howell, Jacoby, Seegmiller & Zannoni, 1962), it was necessary to develop a sensitive assay procedure to measure histidine oc-deaminase (L-histidine ammonia-lyase, EC 4.3.1.3), the enzyme that converts histidine into urocanic acid. The application of this method has show...

Journal: :The Arabidopsis Book 2011

Journal: :Journal of Biological Chemistry 1941

Journal: :Journal of bacteriology 1969
J S Kovach M A Berberich P Venetianer R F Goldberger

Kinetic studies on repression of the enzymes for histidine biosynthesis in Salmonella typhimurium showed that, upon addition of histidine to a derepressed culture, the enzymes became repressed in a temporal sequence which corresponds with the positional sequence of the genes in the histidine operon. This serial pattern of repression occurred under conditions in which the feedback site of the fi...

2014
Nigel J. KILBY

In addition to the primary use of canola in oil pressing, canola is important as a feed supplement for livestock. We have developed a new approach (termed PiggyBackTM expression) that can be used to enhance the histidine content of canola protein. Using PiggyBackTM expression (a novel recombinant approach for generically improving the amino acid composition in crop plants) the histidine content...

Journal: :The Journal of clinical investigation 1990
G Charnogursky A M Moses R Coulson M Bernstein C P Carvounis

Studies in vitro have shown that L-histidine increases the hydroosmotic response to vasopressin. We examined whether this phenomenon occurs also in vivo. Homozygous Brattleboro rats (di/di) were fed a regular diet (0.5% histidine) or a diet enriched with histidine and received 1 ng of 1-deamino-8-D-arginine vasopressin (dDAVP) daily. Addition of histidine (1% by weight) increased post-dDAVP uri...

Journal: :The Journal of biological chemistry 1965
S Schlesinger P Scotto B Magasanik

Three different imidazole compounds are known to induce the enzymes that degrade histidine in Aerobackr aerogenes (l-4). Two of them, histidine and urocanate, are, respectively, the substrate and product of the first enzyme, histidine ammonialyase; the third, imidazolepropionate, is a nonmetabolizable analogue of urocanate. Previous studies with this system did not discriminate between the poss...

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