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Biomedical subjects

G Rose

Publications and source records attributed to G Rose.

At least 289 records · Page 16Linked to original sources
PubMed1973

Palmitoyl-coenzyme A synthetase. Mechanism of reaction.

The mechanism of long-chain fatty acid activation catalysed by highly purified microsomal palmitoyl-CoA synthetase was investigated. The kinetics of the overall reaction were found to conform to the Bi Uni Uni Bi Ping Pong mechanism. (18)O was transferred from [(18)O]palmitate to AMP and palmitoyl-CoA exclusively. The enzyme intermediate formed appeared to consist of enzyme-bound palmitate; this formation occurred only in the presence of ATP. However, the involvement of palmitoyl-AMP in the reaction catalysed by the purified enzyme has proved difficult to establish.

Adenosine Triphosphate↗
PubMed1973

Rat liver microsomal palmitoyl-coenzyme A synthetase. Structural properties.

The structural properties of purified palmitoyl-CoA synthetase from rat liver microsomal material were investigated. The active enzyme has a molecular weight of 168000 and contains about 8.2mol of phospholipid bound/mol of enzyme protein, as well as bound fatty acids. Association of the active enzyme was shown to occur, without impairment of catalytic activity. The lowest-molecular-weight species obtained under denaturing conditions was 27000 daltons.

Amino Acids↗
PubMed1973

Palmitoyl-coenzyme A synthetase. Isolation of an enzyme-bound intermediate.

An enzyme-bound intermediate of the overall reaction catalysed by rat liver microsomal long-chain fatty acyl-CoA synthetase is described. It was found to contain equimolar amounts of adenylate and fatty acid moieties bound to protein, and was stabilized by ATP. The intermediate reacted with CoA to give palmitoyl-CoA.

Adenosine Monophosphate↗
PubMed1972

Microsomal palmitoyl coenzyme A synthetase from rat liver. Partial and exchange reactions.

The partial and exchange reactions of long-chain fatty acid activation were determined by using purified microsomal long-chain fatty acyl-CoA synthetase (EC 6.2.1.3). No significant ATP formation from palmitoyl-AMP and PP(i), nor palmitoyl-AMP-dependent CoA disappearance could be demonstrated. Similarly, no palmitate-dependent [(32)P(2)]PP(i)-ATP exchange was catalysed by the pure enzyme. The above partial and exchange reactions were, however, catalysed by the parent microsomal fraction at a rate similar to that of the overall reaction. The implications of these results are discussed.

Adenosine Monophosphate↗
PubMed1971

The purification and properties of microsomal palmitoyl-coenzyme A synthetase.

The isolation and purification of palmitoyl-CoA synthetase from rat liver microsomes is described. Several methods suitable for enzyme assay are described. The general properties and kinetic parameters of the purified enzyme were determined and are discussed in relationship to microsomal fatty acid activation.

Albumins↗
PubMed1971

Hypertension.

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Adult↗