PubMed Health⌕ Search

Biomedical subjects

R E Merrill

Publications and source records attributed to R E Merrill.

15 recordsLinked to original sources
PubMed1994

On trust.

Explore the source record for details and available documents.

Humans↗
PubMed1991

On physicians and litigation.

Because litigation involving physicians has come to influence the practice of medicine in several ways, we describe many of the legal processes involved. We also offer specific advice in regard to steps which can be effectively taken, and those which should be avoided. We close with a plea for active participation by physicians in the judicial process and in the promulgation of appropriate legislation.

Expert Testimony↗
PubMed1981

Interaction of aromatic dyes with the coenzyme A binding site of choline acetyltransferase.

The interaction of a series of aromatic dyes with the coenzyme A binding site of choline acetyltransferase was studied. Several of the dyes were very potent inhibitors of the enzyme. With few exceptions, inhibition was competitive with respect to acetylcoenzyme A and noncompetitive with respect to choline. It appears likely that inhibition by dyes such as Reactive Blue 2 (Cibacron Blue F3GA) or Congo Red, as in the case of coenzyme A interactions, involves hydrophobic bonding, as well as a coulombic interaction with an arginine residue.

Animals↗
PubMed1981

Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.

Choline acetyltransferase (acetyl-CoA:choline O-acetyltransferase, EC 2.3.1.6) may be inactivated by arginine-specific reagents such as butanedione, phenylglyoxal, and camphorquinone-10-sulfonic acid. The enantiomers of the latter compound were prepared, but inactivation was not stereospecific. Protection against inactivation by the arginine-specific reagents was provided by CoA and, to a lesser extent, by 3'-dephospho-CoA. No protection was provided by choline, NAD+, NADH, NADP+, or NADPH. Sodium chloride could protect, to some extent, against inactivation by arginine-specific reagents; this protection showed no cation or anion specificity. The data are compatible with the postulate that the salt anion competes with the attachment of the 3'-phospho group of CoA to an active site arginine residue.

Acetyl Coenzyme A↗