Results 1 to 10 of about 2,535 (131)

La L-glutamate-1-carboxy-lyase des Pervenches indigènes [PDF]

open access: bronzeBulletin de la Société Botanique de France, 1975
ResumeLes variations de l'acide glutamique et de l'acide γ;-aminobutyrique libres au cours de la vegetation ne sont pas directement superposables a celles de l'activite de la glutamate decarboxylase. Ces dernieres sont dues aux variations de la synthese de l'enzyme.
Pierre Cillard   +2 more
openalex   +3 more sources

Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties [PDF]

open access: greenBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
1. Uroporphyrinogen carboxy-lyase (EC 4.1.1.d), the enzyme catalysing the decaroxylation of uroporphyrinogen to coproporphyrinogen, has been isolated from normal chicken erythrocytes. The enzyme was purified 220-fold with a yield of 24% from haemolysate supernatant by DEAE-cellulose batch treatment, (NH4)2SO4 fractionation and chromatography on DEAE ...
J.M. Tomio   +3 more
openalex   +6 more sources

Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase.

open access: hybridJournal of Biological Chemistry, 1977
DEAE-cellulose chromatography of partially purified preparations of UDP-glucuronate carboxy-lyase from wheat germ results in the separation of two forms of the enzyme. Both are fully active in the absence of added DPN, have indistinguishable molecular weights (210,000), but differ in charge and kinetic properties.
K. V. John   +2 more
openalex   +4 more sources

Porphyria‐induced hepatic porphyrinogen carboxy‐lyase inhibitor and its interaction with the active site(s) of the enzyme [PDF]

open access: bronzeIUBMB Life, 1999
AbstractPorphyrinogen carboxy‐lyase is an enzyme that sequentially decarboxylates uroporphyrinogen III (8‐COOH) to yield coproporphyrinogen III (4‐COOH). In mammals this enzyme activity is impaired by hexachlorobenzene treatment, through generation of an enzyme inhibitor.
S Billi de Catabbi   +4 more
openalex   +5 more sources

Purification and cDNA Cloning of UDP-d-Glucuronate Carboxy-lyase (UDP-d-xylose Synthase) from Pea Seedlings [PDF]

open access: bronzePlant and Cell Physiology, 2002
Uridine diphospho-D-glucuronate carboxy-lyase (UDP-D-xylose synthase; EC 4.1.1.35), which catalyzes the conversion of UDP-D-glucuronate to UDP-D-xylose, was purified to apparent homogenity from pea (Pisum sativum L.) seedlings. The pH optimum for enzyme activity was around 5-6, and the activity was not affected by exogeneously supplied NAD+ and NADH ...
Masaru Kobayashi   +4 more
openalex   +4 more sources

Porphyrins and porphyrinogen carboxy-lyase in hexachlorobenzene-induced porphyria [PDF]

open access: greenBiochemical Journal, 1977
1. Qualitative and quantitative studies of the porphyrins and the porphyrinogen carboxylyase of the liver, spleen, kidney, harderian gland and erythrocytes from normal rats and from those hexachlorobenzene-induced porphyria were carried out. 2. Hexachlorobenzene has no effect on erythrocyte porphyrin content, but produces a decrease in that of ...
Leonor C. San Martín de Viale   +3 more
openalex   +4 more sources

Classificação do diabete melito Diabetes mellitus classification

open access: yesArquivos Brasileiros de Cardiologia, 2010
A correta classificação do diabete melito (DM) permite o tratamento mais adequado e compreende quatro categorias: DM tipo 1; DM tipo 2; Outros tipos e Diabete Gestacional.
Jorge de Faria Maraschin   +3 more
doaj   +1 more source

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