Search PubMed⌕ Search

Biomedical subjects

A M Simon

Publications and source records attributed to A M Simon.

35 records · Page 2Linked to original sources

Multiple forms of rat kidney L-arginine:glycine amidinotransferase.

The relative amount of L-arginine:glycine amidinotransferase (transamidinase) protein in kidneys from rats fed a complete purified diet with and without the addition of creatine and/or glycine was determined by a monoclonal antibody-immunosorbent inhibition assay. Kidneys from the creatine-fed rats had 10% of the transamidinase activities and 78% of the monoclonal antibody immunoreactive transamidinase protein as kidneys from the control rats. An excellent correlation between transamidinase activities and protein was reported previously when the amounts of enzyme protein were determined by immunotitration with polyclonal antibodies. One possible explanation for the contrasting results was that multiple forms of transamidinase are present in rat kidneys. If so, the monoclonal antibody may have recognized forms of the enzyme that were not decreased in amounts commensurate with the decrease in enzyme activities as a result of creatine feeding. Evidence is presented in this report that multiple forms of transamidinase are present in rat kidneys. The distribution of the isoelectric points of the individual forms of transamidinase in kidneys of the control rats appeared to be dissimilar from that in the creatine-fed rats. Therefore, an alteration in the distribution of the individual forms of the enzyme may be a factor in the alteration of transamidinase activities in creatine-fed rats.

Amidinotransferases↗

The purification and characterization of human kidney L-arginine:glycine amidinotransferase.

Human kidney L-arginine:glycine amidinotransferase (transamidinase) has been purified to a homogeneous state as defined by native and sodium dodecyl sulfate gel electrophoresis and by ultracentrifugation (sedimentation equilibrium) experiments. The four steps in the isolation procedure were chromatography with DEAE-cellulose, gel filtration with Sephadex G-150, chromatography with phenyl Sepharose, and high-pressure liquid chromatography with hydroxylapatite. The final product represented a 90-fold purification of the enzyme. Human kidney transamidinase is a dimer with a molecular mass of 89,000 Da and subunit masses of 44,000 Da. The Km for arginine and glycine were both 2.5 mM and the Vmax was 0.5 mumol ornithine/min/mg protein. The ultraviolet absorption spectrum, specific activity, and isoelectric points were determined for human kidney transamidinase. Multiple forms of the enzyme were obtained by isoelectric focusing. Human kidney transamidinase cross-reacted with polyclonal antibodies raised to rat kidney transamidinase. All of the properties of human kidney transamidinase that we have examined were similar to those of rat kidney transamidinase. A close evolutionary relationship between the rat and human kidney transamidinase is suggested.

Amidinotransferases↗

A study of drug abuse in a group of South African university students.

Seventeen informal interviews and 1597 questionnarie responses provided an investigation of drug abuse in a group of South African students. Legal problems in South Africa make research of drug abuse (and indeed many other areas of social relations), particularly interviewing, extremely hazardous and therefore uncommon. Not surprisingly, in view of this, the interviews revealed findings inconsistent with the questionnaire data in many areas. Indeed, the informal technique demonstrated the need for more personal research in this field rather than grouped data questionnaires, the latter being seemingly responsible for the myth of the stereotypic drug taker.

Adolescent↗

Mouse seminal vesicle secretory protein of 99 amino acids (MSVSP99): characterization and hormonal and developmental regulation.

Polyclonal antibodies have been generated to investigate the localization, tissue and species distribution, androgen regulation, and ontogeny of a protein secreted by mouse seminal vesicle, designated as MSVSP99 (ie, mouse seminal vesicle secretory protein of 99 amino acids). MSVSP99 is a polymorphic compound with a molecular weight of around 14 kilodaltons and a positive immunoreactivity range of 5.23 to 5.70. Positive immunoreactivity was restricted to the epithelial cells of the seminal vesicle. Western blot analysis showed organ specificity for MSVSP99, which could not be detected in several organs in the mouse. Time course decrease of MSVSP99 after castration closely followed that of its mRNA. In contrast, the length of time required to restore control levels after testosterone treatment was higher for the protein than it was for its mRNA. Whereas the MSVSP99 gene is already active in 10-day-old males, MSVSP99 is first detected at 27 days. Then, we conclude that factors other than the accumulation of the mRNA regulate MSVSP99 expression.

Amino Acid Sequence↗