Mechanism of release of norepinephrine from peripheral adrenergic neurones by the calcium ionophores X 537A and A 23187.
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Animals↗
Biomedical subjects
J Moss
Publications and source records attributed to J Moss.
Effects of halothane on plasma catecholamines.
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Adrenal Glands↗
Scorpion toxin-induced catecholamine release from synaptosomes.
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Animals↗
Hepatocellular carcinoma and partial deficiency of alpha-1 antitrypsin (MZ).
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Aged↗
Acetyl coenzyme A carboxylase.
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Acetyl-CoA Carboxylase↗
Letter: Alpha-fetoprotein in hepatitis.
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Fetal Proteins↗
On the mechanism of scorpion toxin-induced release of norepinephrine from peripheral adrenergic neurons.
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Animals↗
Catecholamines and hypertension.
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Adrenal Glands↗
Scorpion venom-induced discharge of catecholamines accompanied by hypertension.
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Animals↗
Molecular and catalytic properties of cytosolic acetoacetyl coenzyme A thiolase from avian liver.
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Acetyl Coenzyme A↗
Acetyl coenzyme A carboxylase. Purification and properties of the bovine adipose tissue enzyme.
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Adipose Tissue↗
Acetyl coenzyme A carboxylase. IV. Biotinyl prosthetic group-independent malonyl coenzyme A decarboxylation and carbosyl transfer: generalization to other biotin enzymes.
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Allosteric Regulation↗
Acetyl coenzyme A carboxylase. 3. Further studies on the relation of catalytic activity to polymeric state.
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Adenosine Triphosphate↗
Multiple cytosolic forms of hepatic beta-hydroxy-beta-methyglutaryl CoA synthase: possible regulatory role in cholesterol synthesis.
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Acetoacetates↗
The biotin-dependent enzymes.
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Acetyl-CoA Carboxylase↗
The carboxyl transferase component of acetyl CoA carboxylase: structural evidence for intersubunit translocation of the biotin prosthetic group.
An essential protein component of acetyl CoA carboxylase, isolated and extensively purified from cell-free extracts of Escherichia coli, has been identified as malonyl CoA: d-biotin carboxyl transferase. This enzyme, which does not contain covalently-bound biotin, catalyzes carboxyl transfer from malonyl CoA to free d-biotin, a model reaction for the second step in the carboxylation of acetyl CoA. The transcarboxylation product, after stabilization by methylation, was identified as 1'-N-carboxy-d-biotin dimethyl ester. These results indicate the presence of a biotin site on the carboxyl transferase, distinct from that on the biotin carboxylase, which carries out the first step in the overall process. In addition, the carboxyl transferase catalyzes a slower abortive decarboxylation of malonyl CoA, thus indicating that carboxyl abstraction and protonation do not require the participation of biotin. It is now evident that the half-reactions of acetyl CoA carboxylation are catalyzed by biotin carboxylase and carboxyl transferase. Both components are devoid of biotin and have specific binding sites for free d-biotin, as well as for their respective substrates; hence, the acetyl CoA carboxylation mechanism must involve intersubunit translocation of the carboxylated biotinyl group, which is bound covalently to carboxyl-carrier-protein, a noncatalytic polypeptide.
Bacterial Proteins↗