Industrial sanitation and the role of nurses.
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Humans↗
Biomedical subjects
M K Joseph
Publications and source records attributed to M K Joseph.
Isolation and partial characterization of rat urinary esterase A2.
An enzyme, esterase A2, which hydrolyzes tosyl-arginine methyl ester was isolated from the urine of female, inbred, Dahl-salt-resistant rats using DEAE-Sephadex ion-exchange, aprotinin-agarose affinity and molecular sieve column chromatography. The purest preparation obtained showed four closely migrating bands on polyacrylamide gel electrophoresis. All four bands of the esterase A2 preparation had enzyme activity since all were stainable on zymograms using N-acetyl-L-methionine alpha-naphthyl ester as substrate. Three of these four bands showed decreased electrophoretic mobility following treatment with neuraminidase, indicating that variable sialic acid content accounts for part of the microheterogeneity. The preparation of esterase A2 used was free of rat urinary kallikrein as shown by radioimmunoassay, electrophoretic and isoelectric focusing experiments. The relative kinin-generating ability of rat urinary kallikrein and esterase A2 was highly dependent on the assay used. Using canine plasma as a source of kininogen and the rat uterus to bioassay kinins, esterase A2 was 47% as active as kallikrein; using pure bovine low-molecular-weight kininogen and a radioimmunoassay to measure generated kinins, esterase A2 was only 6% as active as kallikrein. Esterase activity of A2 was activated non-specifically by proteins and detergents. Esterase A2 was 50% inhibited by an 8-fold molar excess of aprotinin and by a 26.5-fold molar excess of soybean trypsin inhibitor, but ovomucoid inhibitor was not inhibitory.
Animals↗
Switching of beta- to alpha-tubulin phosphorylation in uterine smooth muscle of parturient rats.
Proteins from pregnant rat uterine myometrium, previously incubated in the presence of (32P)orthophosphate, were analyzed by one- and two-dimensional polyacrylamide gel electrophoresis and subsequent autoradiography. Electrophoretic patterns of Coomassie blue-stained proteins in preterm and labor myometria were indistinguishable. However, radioactivity incorporated into tubulin in preterm myometrium was predominantly associated with the beta-subunit, whereas in labor, the alpha-subunit was labeled. Endogenous phosphorylated alpha- and beta-tubulins were clearly identified on two-dimensional gel electrophoretograms by apparent molecular weights, isoelectric points, co-migration with marker brain tubulin, and reactivity to specific antitubulin antibodies. The antibodies were incubated with nitrocellulose sheets onto which the myometrial proteins were electrophoretically transferred from the two-dimensional gels. The switching in phosphorylation of beta- to alpha-tubulin in the labor myometrium appears to be a manifestation of estrogen action. The labor-specific phosphorylation changes occurred in parallel with changes in serum estradiol/progesterone ratios. Indeed, estrogen administered to ovariectomized rats caused the appearance of phosphorylated alpha-tubulin, and this effect was inhibited by progesterone. Although the significance of tubulin phosphorylation is not currently understood, the switching in phosphorylation from beta- to alpha-tubulin under estrogen domination may help clarify the role of microtubule phosphorylation.
Animals↗
Modification of RNA polymerase from Escherichia coli by pre-early gene products of bacteriophage T5.
RNA polymerase from cells of Escherichia coli infected with T5 were recovered as a complex with two pre-early phage-coded polypeptides, the 60,000-dalton product of gene A1 and a previously reported 11,000-dalton polypeptide. This RNA polymerase complex had altered transcriptional specificity, in that it transcribed pre-early genes less efficiently than it did early genes.
DNA-Directed RNA Polymerases↗
Idiopathic retroperitoneal fibrosis.
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Adult↗
Proteins binding to kallikrein and esterase A2 in the urine of salt-sensitive and salt-resistant rats.
Iodine-labeled ([125I]) rat urinary kallikrein and rat urinary TAME esterase A2 were used as probes to look for urinary and plasma proteins that bind to these enzymes. Such proteins are presumptive enzyme inhibitors. Complexes formed with labeled enzymes were identified by polyacrylamide gel electrophoresis followed by autoradiography. Urine from young (6 weeks old) Dahl salt-sensitive (S) rats showed no, or only traces, of protein binding to kallikrein. Concomitant with the slow development of hypertension and proteinuria in S rats fed normal rat chow, one of the six kallikrein-binding proteins demonstrable in plasma was readily found in S-rat urine. This kallikrein-binding protein was called "KBP-1." R rats showed either no or much less KBP-1 in the urine, compared to S rats up to 5 months of age. A partly purified preparation of KBP-1 was shown to inhibit the TAME esterase activity of rat urinary kallikrein in the radiometric TAME assay. Urine of proteinuric S rats also contained two TAME esterase-binding proteins, TEBP-1 and TEBP-2, detected with the [125I]-esterase A2 probe. As S rats aged from 3 to 8 months, free KBP-1 disappeared from the urine in spite of increased and marked proteinuria and the continued presence of KBP-1 in plasma. Concomitant with this age-related loss of urinary KBP-1 there was a marked shift in S urinary proteins binding to [125I]-esterase A2 from TEBP-1 to TEBP-2. It was speculated that KBP-1 and TEBP-1 were the same protein detectable with either labeled kallikrein or labeled esterase A2. The concomitant disappearance of free KBP-1 (TEBP-1) and the appearance of free TEBP-2 in the urine of old, hypertensive, proteinuric S rats suggests that: 1) most of the KBP-1 (TEBP-1) is bound to enzyme(s) in old rats; or 2) KBP-1 (TEBP-1) is largely converted to TEBP-2 in old rats; or 3) both are true and that binding of KBP-1 (TEBP-1) to enzymes is associated with the generation of TEBP-2.
Animals↗
Abrogation of G2 checkpoint specifically sensitize p53 defective cells to cancer chemotherapeutic agents.
BACKGROUND: Chkl is a checkpoint gene that is activated after DNA damage. It phosphorylates and inactivates Cdc25C at the late G2 phase. The inactivation of Cdc25C and consequently, the inactivation of Cdc2, are required for the G2 arrest induced by DNA damage. METHODS: We treated 184B5 cell line and its E6 transformed cell lines with adriamycin in the presence of staurosporine or UCNO1 and examined G2 arrest and cell death. RESULTS: We found that adriamycin induced a p53 and p21 response as well as a G1 arrest in 184B5 cells, but not in its E6 transformed cells. Staurosporine or UCNO1 abrogated the G2 arrest induced by adriamycin in both cell lines. In addition, staurosporine or UCNO1 specifically sensitized p53 incompetent cells to adriamycin. CONCLUSION: G2/M checkpoint abrogators can potentially enhance the cytotoxic effect of conventional chemotherapeutic reagents specifically to tumor cells.
Alkaloids↗