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Biomedical subjects

A Bdolah

Publications and source records attributed to A Bdolah.

59 records · Page 4Linked to original sources
PubMed1968

Uridine diphosphate D-glucose dehydrogenase of Aerobacter aerogenes.

Uridine diphosphate d-glucose dehydrogenase (EC 1.1.1.22) from Aerobacter aerogenes has been partially purified and its properties have been investigated. The molecular weight of the enzyme is between 70,000 and 100,000. Uridine diphosphate d-glucose is a substrate; the diphosphoglucose derivatives of adenosine, cytidine, guanosine, and thymidine are not substrates. Nicotinamide adenine dinucleotide (NAD), but not nicotinamide adenine dinucleotide phosphate, is active as hydrogen acceptor. The pH optimum is between 9.4 and 9.7; the K(m) is 0.6 mm for uridine diphosphate d-glucose and 0.06 mm for NAD. Inhibition of the enzyme by uridine diphosphate d-xylose is noncooperative and of mixed type; the K(i) is 0.08 mm. Thus, uridine diphosphate d-glucose dehydrogenase from A. aerogenes differs from the enzyme from mammalian liver, higher plants, and Cryptococcus laurentii, in which uridine diphosphate d-xylose functions as a cooperative, allosteric feedback inhibitor.

Alcohol Oxidoreductases↗
PubMedDate not supplied

Endothelins and sarafotoxins: effects on motility, binding properties and phosphoinositide hydrolysis during the estrous cycle of the rat uterus.

The effects of four peptides of the endothelin/sarafotoxin (ET/SRTX) family on the motility of the rat uterus were examined during the different stages of the estrous cycle. ET-1, ET-3, SRTX-b and SRTX-c showed similar effects on the contraction of the uterus: a slight increase in the maximum tension of the spontaneous rhythmic contractions, a suppression of the relaxation phase of these contractions and an increase in their rate. All three effects were concentration dependent. Of the four peptides, ET-1 and SRTX-b showed the highest potency and efficacy, suggesting that among the various peptides of this family so far studied, ET-1 and SRTX-b are the two full agonists. The rank order of susceptibility of the different stages was, in most cases: proestrus greater than estrus greater than metestrus. Freshly excised diestrus uteri showed no spontaneous contractions and did not respond to any of the peptides. The binding potency of ET-1 and SRTX-b to uterine membranes was similar at the various estrous stages, but their maximal binding decreased gradually from proestrus to diestrus. All four peptides induced phosphoinositide (PI) hydrolysis in uterine slices at all four different stages, with ET-1 and SRTX-b again being more potent than ET-3 or SRTX-c. The maximal PI hydrolysis correlated with the increased rate of the rhythmic contractions. It is suggested that the reaction of the rat uterus to the ET/SRTX peptides depends on its hormonal status and that ET may act in concert with steroid hormones in the modulation of the estrous cycle.

Animals↗