Search PubMed⌕ Search

Biomedical subjects

G Rose

Publications and source records attributed to G Rose.

At least 307 records · Page 17Linked to original sources
PubMed1970

Controlled trial of prednisone in adult patients with the nephrotic syndrome.

A multi-centre controlled trial of steroid treatment of the nephrotic syndrome was carried out on 125 patients. Of these, 64 were controls and 61 received prednisone in a recommended dose range of 20-30 mg./24 hours. The actual initial dose averaged 29 mg./24 hours. Treatment was continued for a variable period, but not less than six months. More than 10 mg./24 hours was given on average for 12 months to all patients, and for longer periods to some. Patients were classified, on the basis of biopsy specimens, into three groups: A, minimal change; B, membranous nephropathy; and C, proliferative glomerulonephritis. In groups B and C prednisone did not have any strikingly favourable effect on proteinuria or on renal function as compared with the control group. In group A, however, prednisone reduced proteinuria to a striking and statistically significant extent. It had little if any effect on long-term renal function in any group. The death rate was higher in the combined prednisone groups (17/61) than in the control groups (12/64). This difference was not statistically significant, but there was a significantly higher number of deaths from cardiovascular disease in the prednisone group, whereas the numbers of deaths from renal failure were not significantly different in the two groups.

Adolescent↗
PubMed1968

Studies on medium-chain fatty acyl-coenzyme a synthetase. Purification and properties.

1. Medium-chain fatty acyl-CoA synthetase (EC 6.2.1.2) was isolated by the method of Mahler, Wakil & Bock (1953) and the enzyme activity determined by the disappearance of CoA in the presence either of butyrate and ATP or of butyryl-AMP, as well as by ATP formation from butyryl-AMP and PP(i). 2. Preincubation of the enzyme with CoA and ATP alone or together, followed by the removal of these substrates by gel filtration, caused a marked inhibition of ATP formation, contrary to results previously obtained with palmitoyl-CoA synthetase. 3. The effect of ATP on butyryl-AMP-dependent CoA disappearance was inconsistent. Low concentrations of ATP (0.1-0.5mm) always caused inhibition, whereas higher concentrations (5-10mm) activated in some enzyme preparations and inhibited in others. 4. This inconsistency was shown to be due to the presence of two enzyme fractions. Both fractions had similar activities when assayed by the butyryl-AMP- or butyrate-plus-ATP-dependent CoA disappearance. However, fraction I was activated by ATP as measured by butyryl-AMP-dependent CoA disappearance whereas fraction II was inhibited by it. Fraction I also catalysed ATP formation from butyryl-AMP and PP(i) whereas fraction II was lacking in such activity. 5. The relationship of these observations with respect to other known mechanisms of fatty acid-activating systems is discussed.

Adenine Nucleotides↗
PubMed1968

Studies on medium-chain fatty acyl-coenzyme a synthetase. Enzyme fraction I: mechanism of reaction and allosteric properties.

1. The mechanism of butyrate activation catalysed by an enzyme fraction derived from ox liver particles (fraction I; Bar-Tana, Rose & Shapiro, 1968) was studied by an analysis of the initial-velocity pattern of the overall reaction and found to conform to the Bi Uni Uni Bi Ping Pong model (Cleland, 1963a,b,c) in agreement with the reaction scheme proposed by Berg (1956). 2. A homotropic co-operative effect was exerted by CoA on fraction I, whereas ATP and AMP functioned as heterotropic co-operative ligands with respect to butyryl-AMP-dependent CoA disappearance. On the other hand, PP(i) and butyryl-CoA showed antagonistic heterotropic effects when tested under similar conditions. With respect to the overall reaction CoA and ATP could be shown to function as co-operative homotropic modifiers. 3. Two interchangeable conformational states of the enzyme are therefore presumed to exist, state R, having a higher affinity for CoA and ATP and thus preferentially catalysing butyryl-AMP-dependent CoA disappearance (partial reaction b), and state T, favoured by the presence of PP(i), catalysing the formation of ATP from butyryl-AMP and PP(i) (partial reaction a) with greater efficiency. 4. These findings serve to explain the opposite effects of ATP on the partial reactions, as well as the inhibition by CoA and ATP of ATP formation (reaction a) and by PP(i) of the butyryl-AMP-dependent CoA disappearance (reaction b) (Bar-Tana et al. 1968). 5. The possible analogy of these observations to amino acid-activating and other similar systems is discussed.

Adenine Nucleotides↗
PubMed1968

Studies on medium-chain fatty acyl-coenzyme a synthetase. Enzyme fraction II: mechanism of reaction and specific properties.

1. The mechanism of reaction of fatty acyl-CoA synthesis catalysed by fatty acyl-CoA synthetase from ox liver (fraction II; Bar-Tana, Rose & Shapiro, 1968) was investigated by a kinetic study of CoA disappearance dependent on butyrate plus ATP or butyryl-AMP (overall and partial reaction b respectively). 2. Contrary to findings with another enzyme (fraction I), a Bi Uni Uni Bi Ping Pong mechanism (Cleland, 1963a,b,c) corresponding to Berg's (1956) scheme of reaction was eliminated and an ordered Ter Ter mechanism with an A-C-B (standing for ATP, CoA and butyrate respectively) sequence of substrate entry for the overall reaction was established for fraction II. Partial reaction (b) was found to follow the ;Iso-Theorell-Chance' mechanism. 3. Also, in contrast with results obtained with fraction I, no allosteric properties could be demonstrated with fraction II.

Adenine Nucleotides↗