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W Albers

Publications and source records attributed to W Albers.

5 recordsLinked to original sources
PubMed1992

The production of fatty acid modifying enzyme (FAME) and lipase by various staphylococcal species.

Eighty-six strains encompassing 11 species of coagulase-negative staphylococci were examined for the production of fatty acid modifying enzyme (FAME) and lipase. Staphylococcus schleiferi and S. saprophyticus most closely resembled S. aureus in that 80% of the strains produced both enzymes. In contrast, no strains of S. lugdunensis and S. haemolyticus tested produced these enzymes. S. simulans was unusual in that eight of 10 strains produced FAME, but only one produced lipase. Among the other species the proportion of strains producing both enzymes ranged from 10 to 60%. Generally there was a strong correlation between FAME and lipase production.

Acyltransferases↗
PubMed1990

Design methods for some dose-response models.

A recently described design method for one-parameter biomedical models such as limiting or serial dilution assays is generalized to two-parameter models for which the dose-response relationship can be expressed as a linear regression model with parameters alpha (intercept) and beta (slope). Design formulae are proposed for three different cases in which prior information about the unknown regression parameters alpha and beta is available (alpha known, beta known and neither known, respectively). A suitable transformation of the two-parameter model enables the direct application of the one-parameter design method to the first two cases, while the third needs more advanced considerations. Two experimental designs, taken from the literature, are reproduced as closely as possible using the methods described, thus showing under which circumstances these designs are suitable.

Animals↗
PubMed1977

A-V block.

Explore the source record for details and available documents.

Atrioventricular Node↗
PubMed1975

Sodium + potassium-activated ATPase of mammalian brain. Regulation of phosphatase activity.

1. The K+-nitrophenylphosphatase activity associated with mammalian brain (Na+ + K+)-ATPase displays K+ activation curves that have intermediary plateaus and maxima in the presence of less than saturating concentrations of Na+. Zero Na+ and saturating Na+ produce sigmoid K+-activation curves with low and high K+ affinities respectively. 2. ATP inhibits K+-activated nitrophenylphosphatase through both competitive and non-competitive mechanisms. ATP is synergistic with Na+ in the mechanism which converts the enzyme from low to high K+ affinity. 3. The Na+ and K+ interactions can be accounted for by equations which describe a model with separate regulatory sites for Na+ and K+ and with K+- requiring catalytic site which is only accessible in one of the two principal conformational stages of the enzyme. 4. The effects of ATP can be accounted for by the same model through interactions at a single nucleotide binding site. Inhibition which is competitive with K+ and non-competitive with substrate arises from stabilization of the inactive enzyme conformation. Inhibition which is non-competitive with K+ and competitive with substrate results from interactions with the active enzyme conformation. The synergism between Na+ and ATP appears to arise as a consequence of the formation of phosphoryl enzyme. 5. A model for (Na+ + K+)-ATPase is discussed which involves in-phase coupling of subunit interactions as suggested by these studies.

Adenosine Diphosphate↗