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Biomedical subjects

G M Steinberg

Publications and source records attributed to G M Steinberg.

18 recordsLinked to original sources

Dextrality and eye position in putting performance.

The relationship between eye and hand dominance and the relative positioning of the ball with respect to the subjects' eyes on putting performance was investigated. Twenty-four pure dextral (right-eyed and right-handed) and 24 cross-dextral (left-eyed and right-handed) novice golfers were randomly assigned to putt at a target 3.66 m away in two conditions, eyes focused directly over the ball and eyes positioned midway between their feet and the ball, i.e., eyes positioned 5 cm closer to their feet. The analysis indicated a significant interaction for dextrality and the relative position of the eyes during putting. Pure dextral golfers demonstrated less absolute error and less variable error in their putting performance when they focused their eyes midway between the ball and their feet than when they positioned their eyes directly over the ball. No differences in error scores were found for cross-dextrals across the two putting conditions.

Adolescent↗

Spontaneous reactivation of acetylcholinesterase following organophosphate inhibition. I. An analysis of anomalous reactivation kinetics.

The first kinetic studies on the spontaneous reactivation of Sarin-inhibited acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) are reported. With increasing pH the extent of reactivation increases while the observed rate constant decreases. An analysis of the change in aging rate constant as a function of pH suggests that the aging of alkyl-alkoxy phosphonylated acetylcholinesterases is not solely acid catalyzed.

Acetylcholinesterase↗

A hydrophobic binding site in acetylcholinesterase.

The dissociation constants have been determined and compared for a series of reversible, noncovalent inhibitors of eel acetylcholinesterase that are structurally related to the very potent inhibitor, 1,2,3,4-tetrahydro-9-aminoacridine (THA). It is concluded that there exists on the enzyme protein, closely adjacent to the anionic subsite, a conformationally flexible, hydrophobic area which tends readily to assume a near planar form. The dimensions of this area are unknown, but it is adequate in size to fully accomodate THA. It is this area, acting conjointly with the adjacent anionic subsite, which provides the attraction for THA and related inhibitors. Uv absorbance maxima and pKa vlaues are reported for many of the compounds.

Acetylcholinesterase↗