Publications by authors named "Marais R"

The substrate specificity of purified PKC-alpha, -beta and -gamma has been investigated. A series of synthetic peptides based upon the sequence surrounding serine-7 in glycogen synthase were generated and used to determine the basic residue requirements of these PKC isotypes. While PKC-alpha and -beta are indistinguishable in their phosphorylation of these peptides, PKC-gamma shows a distinct specificity profile for these synthetic substrates.

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The aim of this study was to compare first-year students enrolled in an Integrated Course at a Nursing College (n = 103) with first-year paramedical students from the following disciplines: Logopaedics (n = 12); Physiotherapy (n = 24); Occupational Therapy (n = 18); BSc Nursing (n = 12); Radiography (n = 27), on the Profile of Mood States (POMS), Health Behaviour Assessment Scale (HBAS) and Matric scores. The Integrated Nursing students revealed significantly lower Matric scores than the other students (p less than 0.0001), and showed significant differences on other variables, indicating higher negative mood states and less healthy life-styles.

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We determined whether the beta or gamma protein kinase C (PKC) subtypes implicated in long-term potentiation (LTP) selectively regulates protein F1 phosphorylation. Purified bovine PKC subtypes and recombinant PKC subtypes activated by phosphatidylserine (PS) and calcium were tested for their relative ability to phosphorylate purified rat protein F1 (a.k.

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The purpose of the present study was to examine protein kinase C (PKC) isotype expression in T lymphoblasts derived from peripheral blood and the T leukaemic cell Jurkat. Using antisera reactive with PKC alpha, beta 1, and beta 2 and gamma, it was observed that T cells expressed two PKC isotypes, PKC alpha and beta 1. No PKC gamma was detected in T lymphocytes.

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The structural analysis of protein kinase C has led to the identification of a family of related gene products. This family of kinases consists of six unique genes that give rise to at least seven polypeptides. The high degree of conservation and the differential distribution of these mRNAs/proteins suggest that they perform distinct functions in vivo.

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As a means of determining the role of protein kinase C in the signal transduction from novel growth factors and hormones, we investigated the effects of well-characterized agents on the phosphorylation state of protein kinase C itself. These studies show that agents that stimulate protein kinase C either directly (phorbol esters) or indirectly through phosphatidylinositol breakdown (platelet-derived growth factor) induce an increase in the phosphorylation state of the kinase. By contrast, epidermal growth factor, which does not stimulate protein kinase C in fibroblasts, does not increase the phosphorylation state of protein kinase C, but leads to a decrease.

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Four monoclonal antibodies (mAbs), derived from high-responder Biozzi mice immunized with purified protein kinase C, were selected by ELISA and further characterized by immunoblot: 3G12, 5A2, 36G9 are of isotype gamma 1, kappa and 15G4 is of isotype gamma 2b, kappa. Competition analysis between 15G4 and the three other mAbs showed that 15G4 and 3G12 are directed against either the same or overlapping epitope(s). All four mAbs are specific for the bovine gamma isoform of protein kinase C and cross-react with protein kinase C gamma from a variety of animal species.

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Several polyclonal antisera specific for each of the protein kinase C isotypes alpha, beta 1, beta 2 and gamma have been generated and used to monitor the purification and subsequent separation of these polypeptides. A simple protocol has been developed for the efficient co-purification of these isotypes from bovine brain. The separation of the alpha, beta 1, beta 2 and gamma isotypes has been monitored using the antibodies and pools containing pure alpha, beta 1, and gamma forms have been produced.

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Previous studies demonstrated that activation of T lymphocytes by phorbol ester or mitogenic lectin leads to phosphorylation of Ser 126 of the CD3 antigen gamma chain, whereas treatment with ionomycin results in phosphorylation of both Ser 123 and 126 [Davies, A. A. et al.

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The likelihood of bacterial resistance now prevents the use of oxytetracycline in the empirical therapy of anaerobic infections. This study investigates the in-vitro activity of two semi-synthetic derivatives, doxycycline and minocycline, against a range of anaerobic bacteria. MICs for each antibiotic were determined by an agar incorporation technique.

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The in vitro activity of erythromycin and RU-28965 (a novel macrolide antimicrobial with improved pharmacokinetics) was determined against a variety of anaerobic bacteria in anaerobic atmospheres with and without added carbon dioxide. Minimum inhibitory concentrations (MIC) were determined using an antimicrobial incorporation technique in Wilkins-Chalgren agar (Oxoid, UK) containing saponinlysed horse blood to a final concentration of 10%. The inoculum used was approximately 10(4) colony forming units (cfu) contained in 10 microliters Wilkins-Chalgren broth, which was applied to the surface of the agar plates using a multipoint inoculator.

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The in vitro activity of vancomycin and teicoplanin, a new glycopeptide antimicrobial, was determined against a total of 286 anaerobic bacteria including Bacteroides fragilis group (100), B. melaninogenicus (21), B. bivius (16), Fusobacterium spp.

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Four hundred and thirty-six Black and Coloured patients with tuberculosis were examined for diabetes mellitus, which was found in 2,1%. In this series 29% of diabetics with tuberculosis had lower lung field involvement only, while the prevalence of isolated lower lung field tuberculosis among the non-diabetics was only 4,5%. It was therefore concluded that diabetes mellitus should be looked for in patients with isolated lower lung field tuberculosis.

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