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Robert H. Abeles

Researcher at Harvard University

Publications -  8
Citations -  454

Robert H. Abeles is an academic researcher from Harvard University. The author has contributed to research in topics: Cofactor & Reductase. The author has an hindex of 6, co-authored 8 publications receiving 439 citations. Previous affiliations of Robert H. Abeles include Brandeis University & National Institutes of Health.

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A derangement in B12 metabolism leading to homocystinemia, cystathioninemia and methylmalonic aciduria

TL;DR: The results of the investigation of an infant with abnormalities of both the sulfur amino acids and methylmalonic acid indicate the occurrence of a hitherto unrecognized metabolic abnormality, a defective ability to accumulate the coenzymatically active derivatives of B 12 .
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A derangement in B12 metabolism associated with homocystinemia, cystathioninemia, hypomethioninemia and methylmalonic aciduria

TL;DR: According to autopsy, this infant could not adequately metabolize B, and as a result failed to accumulate coenzymatically-active derivatives of vitamin B, in normal amounts, and it is suggested that therapeutic benefit may derive from the administration of forms of 6, that could circumvent the metabolic block, by giving substances that could stimulate the non-B, -dependent methionine-synthesizing system or by the Administration of methamphetamineionine in large doses.
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The Mechanism of Action of Cobamide Coenzyme in the Ribonucleotide Reductase Reaction

TL;DR: The results indicate that cobamide coenzyme functions as an essential hydrogen-transferring agent in the cobamide-dependent ribonucleotide reductase reaction, and that transferred hydrogen attaches to carbon atom 5' of the coen enzyme deoxyadenosyl moiety.
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Modulation of Recombinant Human Prostate-Specific Antigen: Activation by Hofmeister Salts and Inhibition by Azapeptides† Appendix: Thermodynamic Interpretation of the Activation by Concentrated Salts

TL;DR: It is demonstrated that human PSA (rh-PSA) has properties similar to those of native PSA isolated from human seminal fluid and Analytical ultracentifugation and dynamic light scattering indicate that PSA remains monomeric under high-salt conditions.
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The Mechanism of Action of Ethanolamine Ammonia-Lyase, a B12-dependent Enzyme IX. INTERACTION OF THE ENZYME-COENZYME COMPLEX WITH REACTION PRODUCTS

TL;DR: It was concluded that 1-aminoethanol is an intermediate in the reaction, and when NH4+ is omitted, no tritium transfer to acetaldehyde occurs, but the dissociation of the carbon-cobalt bond is accelerated.