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Biomedical subjects

J L Rabinowitz

Publications and source records attributed to J L Rabinowitz.

At least 91 records · Page 5Linked to original sources
PubMed1973

Studies of trans-3-methyl-2-hexenoic acid in normal and schizophrenic humans.

The report that sweat of certain schizophrenics contains the branched chain fatty acid, trans-3-methyl-2-hexenoic acid (TMHA), stimulated an investigation to evaluate the relationship between this fatty acid and schizophrenia. A sensitive and specific gas-liquid chromatography-mass spectroscopic procedure was developed for analyzing biological fluids for TMHA. Analysis of sweat samples from normal and schizophrenic subjects indicated that the sweat of both groups contains comparable quantities of this fatty acid. In addition, the fate of intravenously administered (14)C-labeled TMHA was shown to be similar in normal and schizophrenic subjects. It is concluded that there is no relationship between TMHA and schizophrenia.

Caproates↗
PubMed1971

Thyroxine: convesion to triiodothyronine by isolated perfused rat heart.

Thyroxine labeled with carbon-14 and iodine-125 was perfused through surviving rat hearts. Only when unlabeled triiodothyronine was added as a carrier could the newly formed doubly labeled triiodothyronine be isolated. The fact that this triiodothyronine was labeled with the correct ratio of carbon-14 to iodine-125 indicated that it originated from thyroxine. Approximately 5 percent of the initial carbon-14 radioactivity was found in the recovered triiodothyronine.

Animals↗
PubMed1969

Artificial substrates for prenyltransferase.

Four out of 16 new allylic pyrophosphates synthesized were found to be artificial substrates for liver prenyltransferase (EC 2.5.1.1). These were the trans-and the cis-3-ethyl-3-methylallyl, the 3,3-diethylallyl and the (mixture of cis and trans) 3-methyl-3-n-propylallyl pyrophosphates. The products synthesized from these substrates and isopentenyl pyrophosphate were the appropriate homo- and bishomo-farnesyl pyrophosphates. Substitution of 3,3-dimethylallyl pyrophosphate at C-2 with a methyl group destroyed its reactivity with the enzyme. Neither the unsubstituted allyl pyrophosphate nor the cis- or trans-3-methylallyl pyrophosphate could be condensed with isopentenyl pyrophosphate. Thus the simplest allylic substrate for prenyltransferase is 3,3-dimethylallyl pyrophosphate.

Animals↗