Results 11 to 20 of about 2,753 (185)
La L-glutamate-1-carboxy-lyase des Pervenches indigènes [PDF]
Bulletin 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
openaire +2 more sources
Porphyrin biosynthesis. VII. Porphyrinogen carboxy-lyase from avian erythrocytes. Purification and properties [PDF]
Biochimica 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 ...
Tomio, J.M. +3 more
openaire +5 more sources
UDP-glucuronate carboxy-lyase in cultured chondrocytes.
Journal of Biological Chemistry, 1977 UDP-glucuronate carboxy-lyase has been demonstrated in chick chondrocytes in tissue culture. It occurs in the particulate fraction, and its activity is stimulated by exogenous NAD. The enzyme is allosterically activated by UDP-glucuronate and inhibited by UDP-xylose, n Values of 2.8 indicate positive cooperativity of at least three interacting sites on
K V, John, N B, Schwartz, H, Ankel
openaire +3 more sources
Inhibition of Glutamic Acid Carboxy-Lyase by Alanosine
Experimental Biology and Medicine, 1968 SummaryAlanosine is an inhibitor of glutamic acid carboxy-lyase (C-L) of bacterial origin, but not of those from squash and rat brain. Its action is competitive in respect to glutamic acid, but noncompetitive in respect to pyridoxal phosphate. Other bacterial amino acid C-L's tested, while sensitive to hydroxylamine, are not inhibited by alanosine.
G R, Gale, L M, Atkins
openaire +3 more sources
Porphyria‐induced hepatic porphyrinogen carboxy‐lyase inhibitor and its interaction with the active site(s) of the enzyme [PDF]
IUBMB 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 B, de Catabbi +4 more
openaire +4 more sources
Separation and allosteric properties of two forms of UDP-glucuronate carboxy-lyase.
Journal 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, J S, Schutzbach, H, Ankel
openaire +3 more sources
Porphyrins and porphyrinogen carboxy-lyase in hexachlorobenzene-induced porphyria [PDF]
Biochemical 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 ...
L C, San Martín De Viale +3 more
openaire +4 more sources
Purification and cDNA Cloning of UDP-d-Glucuronate Carboxy-lyase (UDP-d-xylose Synthase) from Pea Seedlings [PDF]
Plant 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
openaire +3 more sources
Effects of Certain Hydroxamic Acids on L-Glutamate 1-Carboxy-lyase
Experimental Biology and Medicine, 1969 SummaryOver 50 hydroxamic acids (HA) were surveyed for inhibitory action against bacterial and vegetable glutamic acid carboxy-lyase (GCL). Appreciable activity against the bacterial enzyme was shown by 7 compounds. These 7, in addition to 2 others, also inhibited the vegetable enzyme.
J A, Howle, G R, Gale
openaire +3 more sources
Appendix-Ultracentrifuge studies on crystalline
Biochemical Journal, 1963 PH Lloyd
openaire +4 more sources