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Biomedical subjects

J F McKelvy

Publications and source records attributed to J F McKelvy.

16 recordsLinked to original sources
PubMed1979

Enzymes involved in the degradation of thyrotropin releasing hormone (TRH) and luteinizing hormone releasing hormone (LH-RH) in bovine brain.

As part of an investigation of neuropeptide inactivation mechanisms, we have resolved an enzymatic activity in bovine brain which catalyzes the deamidation of thyrotropin releasing hormone (TRH) and the hydrolysis of the Pro9--Gly10--NH2 bond of luteinizing hormone releasing hormone (LH-RH) from a second LH-RH degrading activity which does not degrade TRH. The former activity is similar, if not identical to, the post-proline cleaving enzyme in kidney as it is active toward the post-proline cleaving enzyme substrate CbzGly--Pro--Leu--Gly and inhibited by CbzPro--Phe and diisopropylfluorophosphate. In addition, products derived from the degradation of TRH and LH-RH by this activity show a specific cleavage on the carboxyl side of a proline residue. The latter activity has not yet been characterized with respect to its site of cleavage of the LH-RH molecule due to the presence of other contaminating peptidases.

Amino Acid Sequence↗
PubMed1977

Degradation of L-[3H]fucose-labeled plasma membrane components from regenerating rat liver.

The rates of degradation of liver cell plasma membranes from control and partially hepatectomized rats were investigated by a single isotope administration procedure utilizing L-[3H]fucose as a precursor. The label was incorporated maximally into normal plasma membranes at 2 to 4 h after intravenous injection. At 4 h, L-[3H]fucose activity was 8-fold more abundant in membrane protein than in total liver protein. Paper chromatography of neutral sugars liberated by acid hydrolysis of the plasma membranes indicated that greater than 90% of the recovered radioactivity was in the form of fucose. After partial hepatectomy, the wet weight of the right lateral liver lobe increased linearly during a 4-day postoperation interval. In addition, the specific activity of plasma membrane alkaline phosphatase was elevated to a level that remained 3 to 4 times higher than that of the control membranes. However, there was not much difference between the mean rates of degradation of the labeled plasma membrane components from the control and regenerating livers. The apparent half-lives were 33 and 40.8 h, respectively. This suggests that the dissociation of fucose-containing components from the plasma membrane is not markedly altered during the process of rapid compensatory liver growth.

Animals↗
PubMed1976

Binding studies of polypeptide hormones to bovine neurophysins.

Experimental binding isotherms of [9-glycinamide-1-(14)C]oxytocin and [9-glycinamide-1-(14)C]arginine vasopressin to purified neurophysins I and II at pH = 4.4, 5.4, 6.5, 7.4, and 8.5 and 6 degrees, 22 degrees, and 37 degrees in aqueous buffers are reported. For purposes of comparison, binding isotherms for [4-glycine-1-(14)C]oxytocin to neurophysin II and I in aqueous buffer, and [9-glycinamide-1-(14)C]oxytocin to neurophysin II in dimethylsulfoxide under selected conditions are also reported. A brief discussion of the interpretation of binding isotherms is entered into and apparent binding constants are derived. The results indicate that the interpretations presented in the literature up to now are much too simple. There are, in contrast, multiple binding sites of oxytocin and vasopressin to the neurophysins and large temperature dependences of the number of sites and their binding constants. We find, in fact, that at 37 degrees the binding of neurohypophysial hormones to the supposed storage proteins is rather weak even at the pH of maximum binding.

Amino Acids↗
PubMed1976

Preliminary analysis of 1H and 13C spectral and relaxation behavior in methionine-enkephalin.

Nuclear magnetic resonance studies on the conformational dynamics of the pentapeptide H-Tyr-Gly-Gly-Phe-Met-OH are reported. This peptide, for which the generic trivial name "methionine-enkephalin" has been suggested, is pharmacologically active as a ligand for the mammalian opiate receptor(s). The studies reported are parallel investigations in two solvents (dimethylsulfoxide and water) of: 1H and 13C high resolution spectral assignments; 1H and 13C spin-lattice relaxation times, temperature dependence of amide proton chemical shifts, and half-times for chemical exchange or amide protons. From these data we conclude that the tyrosine side chain of methionine-enkephalin exhibits restricted motion with respect to the main peptide backbone of the molecule. On the other hand both the phenylalanyl and methionyl side chains are undergoing intramolecular reorientation with relatively high frequency.

Amides↗
PubMed1975

Isolation and partial characterization of a bile canalicular plasma membrane fraction from normal and regenerating rat liver.

A bile canalicular membrane fraction was isolated from 24-hour regenerating rat livers, and its properties were compared to those of homologous fractions prepared from the livers of sham-operated and unoperated controls. These canalicular membrane fractions were found to be closely related in terms of their morphology, their purity, their yield, and their qualitative protein banding profiles on sodium dodecyl sulfate-polyacrylamide gels. However, when a rigorous examination of plasma membrane enzyme marker activities was made, the regenerating liver membranes were shown to possess an increased specific activity of alkaline phosphatase and lower levels of Mg2+ ATPase and 5'-nucleotidase in comparison with control specific activity values.

Animals↗
PubMed1975

Biosynthesis of thyrotropin-releasing hormone in organ cultures of the guinea pig median eminence.

Guinea pig median eminence tissue was put into organ culture for periods up to 13 days. The cultured tissue was examined in 3 ways at various ages: a) morphologically, by transmission electron microscopy and light microscopic autoradiography; b) biochemically, by determination of the ability of the cultures to accumulate [3H]L-proline and to incorporate this isotope into [3H]TRH; and c) by bioassay, in which the content of TRH in tissue and culture medium was determined by the ability of extracts of both to release radioimmunoassayable TSH from rat hemi-pituitaries incubated in vitro. It was found that the cultures exhibited a high degree of preservation of ependymal cell morphology and a sustained ability to accumulate [3H]L-proline over the entire 13-day time course. Neuronal elements showed a progressive degeneration with time in culture, and the ability of the culture to produce [3H]TRH was lost concomitantly with the loss in neuronal integrity.

Animals↗