Biomedical subjects
Publications and source records attributed to S Ray.
An enzyme from goat plasma which catalyzes the oxidation of aminoacetone to methylglyoxal has been isolated and purified to apparent homogeneity. This enzyme has been found to be identical with the well known amine oxidase. Several properties of the enzyme have also been described.
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The syntheses of (+/-) 2 alpha,6 beta -diethyl-7 alpha -ethynyl-3 alpha-(p-hydroxyphenyl)-trans- bicyclo[4.3.0]nonan-7 beta-ol (8), (+/-)2 beta,6 beta-diethyl-7 alpha-ethynyl-3 beta-(p-methoxy-phenyl)-trans-bicyclo[4.3.0]nonan-7 beta-ol 12 and (+/-) 2 alpha,6 beta-diethyl-7 alpha-ethynyl-3 beta-(p-hydroxyphenyl)- trans-bicyclo[4.3.0]nonan-7 beta-ol (18) and their derivatives, which are essentially B-seco-steroids having cis-anti-trans, cis-syn-trans and trans-anti-trans geometries have been carried out. A study of their antiimplantation activities (AI) and receptor binding affinities (RBA) show that trans-anti-trans compounds are biologically most potent, followed by the corresponding cis-anti-trans and cis-syn-trans compounds. The most potent compound 18 is active at 1 mg/kg in rats. Introduction of 7 alpha-ethynyl group increases their AI activity; however, no significant effect on their RBA is observed.
In a study of the effect of the substituent on the receptor binding affinity (RBA), estrogenicity, and antiimplantation (AI) activity in trans-3,4-diarylchromans, it has been found that demethylation of trans-2, 2-dimethyl-3-phenyl-4-[p-(beta-pyrrolidinoethoxy)phenyl]-7-methoxychroman (centchroman, 1) to the corresponding 7-hydroxy compound (7) results in a 20-fold increase in RBA (112%) without any appreciable change in AI activity. On the other hand, absence of the pyrrolidinoethyl group from the 4-phenyl residue (6) leads to a drop in both RBA and AI activity. A chain length of two to three carbon atoms and a pyrrolidino ring appear to be necessary for activity in these compounds. It has been found that while the trans isomers with the tertiary aminoalkoxy side chain in the para position of the 4-phenyl radical were the most active, in the corresponding cis-chromans and chromenes, analogues with this chain in the meta position were most active; the ortho substituted compounds of all these series were inactive. In 3-phenyl-substituted compounds, the trans isomer carrying the p-hydroxy substituent (33) was found to be the most active; the corresponding pyrrolidinoethyl ether (13) showed a lower order of activity. The implication of these observations on the mapping of the different subsites on the receptor has been discussed.
Two alpha-ketoaldehyde dehydrogenases, one catalyzing the oxidation of methylglyoxal to pyruvate with NAD and the other with NADP, were isolated from goat liver and happened to be co-purified. Both the enzymes had been extensively purified to the point where only these two enzymes were present. By affinity chromatography on a thiol-Sepharose column, the two enzymes were separated. Molecular weight of both the enzymes was found to be 42,000 by gel filtration in a Sephadex G-200 column. Electrophoresis on sodium dodecyl sulfate-polyacrylamide gel revealed that the enzymes are composed of single subunits. Interaction with mercurials indicated the presence of SH group(s) in the active site of the NAD-linked enzyme only.
The effect of different nucleotides and glycolytic intermediates was tested on the NAD-linked and NADP-linked alpha-ketoaldehyde dehydrogenases involved in the oxidation of methylglyoxal to pyruvate. ATP, GTP, and ADP strongly inhibit the NAD-linked enzyme whereas activity of the NADP-linked enzyme remained unaltered. NADP at a concentration much below its catalytic concentration strongly inhibited the NAD-linked enzyme. This NADP inhibition decreased with decreasing of the pH of the incubation medium. Fructose 1,6-bisphosphate stimulated and glyceraldehyde 3-phosphate inhibited the activity of the NAD-linked enzyme whereas dihydroxyacetone phosphate inhibited NADP-linked activity. The stimulatory effect of fructose 1,6-bisphosphate diminished with lowering of the pH value. The various effects by several key metabolites of the glycolytic pathway indicate a possible physiological role for these enzymes.
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Guar gum, a galactomannan, is growth depressing when fed to chicks. As part of the continuing studies on the mode of action of this and other gums in the intestine, a mannanase has been isolated which degrades guar gum. A commercial hemicellulase was separated into several protein fractions by chromatography on DEAE-cellulose. Only one of these proteins effectively reduced the viscosity of a guar gum solution. Activity towards pectin, rye water extract, and barley water extract was not present in the fraction which degraded guar gum but was found in other fractions at lower concentrations. Graded levels of this purified guar-degrading enzyme were incorporated into chick diets having 2% guar gum. This purified enzyme was effective at levels as low as .6 mg protein/kg diet in preventing growth depression caused by the guar gum and thus permitting growth equivalent to controls. Purity of this mannanase was confirmed by chromatography on QAE-Sephadex at pH 6.0 and by slab-gel electrophoresis at pH 8.4.
An enzyme fraction which specifically catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate has been isolated and partially purified from goat liver. The enzyme fraction appears to be substantially free from glyoxalase I, reduced glutathione, and triosephosphate isomerase. Approximately equimolar quantities of methylglyoxal and inorganic phosphate were obtained from dihydroxyacetone phosphate. Formation of methylglyoxal was confirmed by colorimetric and enzymatic estimations as well as by paper chromatography and its spectrum. Glyceraldehyde-3-phosphate, fructose 1,6-bisphosphate, dihydroxyacetone, and glyceraldehyde, failed to act as substrates. The enzyme is inhibited by some phosphorylated compounds and inorganic phosphates.
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The Cratty Test of Gross-Motor Performance was administered to 18 Down syndrome and 18 other mentally retarded children between the ages of 7 and 14 years. Subjects were individually matched on both MA and CA. Examination of their test profiles showed that the Down syndrome children had consistently lower scores that did the matched control children, but only two of the differences were significant. The findings, therefore, provide tentative support for the notion that Down syndrome children suffer a specific deficit in some areas of motor coordination. A number of criticisms of the internal consistency of the test were discussed in terms of their theoretical and practical implications.
Cadmium concentration in Nereis virens exposed to sediment spiked with cadmium increased linearly with time, no equilibrium concentration being indicated by 24 days of exposure. The concentration with N. virens also increased with concentration of Cd in the sediment, and smaller worms accumulated higher amounts per unit weight than larger worms. With exposure to sediment containing 1 to 4 ppm Cd, accumulation rates ranged from 0.018 to 0.037 microgram Cd/g dry wt/hr for 1- to 2-g worms and from 0.014 to 0.024 microgram Cd/g dry wt/hr for 5- to 7-g worms. N. virens exposed to 0.03 to 9.2 ppm Cd in sea water for 14 days had accumulation rates of 0.019 to 2.217 microgram Cd/g dry wt/hr for 1- to 2-g worms and 0.013 to 1.327 microgram Cd/g dry wt/hr for 5- to 7-g worms. There was practically no excretion of cadmium for N. virens with initial concentrations of 5 to 20 microgram Cd/g dry wt during 75 days in clean conditions. Sediment containing 1 and 4 ppm Cd produced concentrations of about 0.03- and 0.1-ppm cd in the overlying water. The accumulation rates from sediment with 1 and 4 ppm Cd are equal to the rates from sea water with 0.03 and 0.1 ppm Cd, respectively, indicating that cadmium uptake by N. virens is primarily from the aqueous phase.
Cadmium uptake rates in various tissues of Pandalus montagui exposed to sea water containing 37 micrograms Cd/L for 14 days ranged from 0.002-0.06 microgram/dry tissue/hr. During depuration for 57 days, the levels in most tissues decreased slightly, but continued to rise in the hepatopancreas indicating Cd redistribution. Exposure to 65 micrograms Zn/L produced no substantial change in Zn content of the tissues. An increase occurred in eggs and hepatopancreas during the first six days of depuration. During exposure to Cd and Zn combined (40 micrograms Cd/L + 70 micrograms Zn/L), tissue Zn levels responded as with Zn alone. In the presence of Zn, Cd concentration was doubled in the hepatopancreas, depressed by one-third in the carcass, and did not change in the other tissues. Increased amounts of Zn (up to 410 micrograms Zn/L) had not effect on the Cd levels of the tissues except that the Cd level in the hepatopancreas was depressed, although the level was still greater than in the case of exposure to Cd alone. The possible role of metallothionein is discussed.
The antihistaminic drug ambodryl (Am) and the tranquillizer promazine (Pr), which had previously shown significant antimicrobial activities, were used to select bacterial mutants representing different levels of resistance to their action. These Am and Pr mutants were found to have simultaneously developed cross-resistance to penicillin (Pe), streptomycin (Sm), chloramphenicol (Cm), tetracycline (Tc) and kanamycin (Km). Certain first-step Am mutants of sensitive wild-type bacteria which were also sensitive to these antibiotics developed resistance to Pe and Sm as well as to Pr and the antihistamine benadryl (Bn). The next-step mutant of Am resistance not only doubled its resistance to these antibiotics and chemotherapeutics, but broadened its resistance-spectrum to cover Tc and Cm. These observations on cross-resistances seem to be best explained on the basis of a reduction in cell-membrane permeability acting in a nonspecific manner. The role of such cross-resistance in accounting for an overall increase in the minimum inhibitory concentrations (MIC) of many drugs against several groups of bacteria is evaluated.
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The most unique property of subchoroidal fluid was found to be the high bilirubin level. One distinct yellow band in the same position as albumin was observed when it was subjected to electrophoresis on agarose film. The yellow compound was very soluble in chloroform. Its identity to bilirubin was confirmed by its absorption maximum at 445 nm, and a positive reaction with Ehrlich's diazo reagent. Subretinal fluid and liquid vitreous often had a yellowish appearance after ocular hemorrhage. However, their bilirubin level was not elevated above that of serum. Our data indicated that the degradation of RBCs may be an important causative factor of persistant detachment.
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