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A M May

Publications and source records attributed to A M May.

10 recordsLinked to original sources

Muscle function during repetitive moderate-intensity muscle contractions in myoadenylate deaminase-deficient Dutch subjects.

We investigated whether the capacity for repetitive submaximal muscle contraction was reduced in a group of subjects (n=8) with a primary deficiency of myoadenylate deaminase (MAD). Quadriceps femoris muscle fatigue was evaluated using voluntary and electrically stimulated contractions during 20 min of repetitive voluntary isometric contractions at 40% of maximal force-generating capacity (MFGC). After 5 min of exercise, MFGC had declined significantly to 70.6+/-4.1% (mean+/-S.E.M.) and 87.2+/-1.6% of baseline values in MAD-deficient and sedentary control subjects (n=8) respectively (P=0.002 between groups). After 5 min of exercise, the half-relaxation time had increased significantly to 113.4+/-6.1% of baseline in MAD-deficient muscle, but had decreased significantly to 94.1+/-1.3% in control subjects (P=0.003 between groups). All control subjects completed the 20-min exercise test. Five of the MAD-deficient subjects had to stop exercising due to early muscle fatigue; however, three of the MAD-deficient subjects were able to complete the 20-min exercise test. In conclusion, although the capacity for repetitive submaximal isometric muscle contractions for the group of MAD-deficient subjects was significantly decreased, it remains uncertain whether MAD deficiency is the sole cause of pronounced muscle fatigue.

AMP Deaminase↗

Betaine synthesis in chenopods: Localization in chloroplasts.

PLANTS FROM SEVERAL FAMILIES (CHENOPODIACEAE, GRAMINEAE, COMPOSITAE) ACCUMULATE BETAINE (GLYCINE BETAINE) IN RESPONSE TO SALT OR WATER STRESS VIA THE PATHWAY: choline --> betainal (betaine aldehyde) --> betaine. Betaine accumulation is probably a metabolic adaptation to stress. Intact protoplasts from leaves of spinach (Spinacia oleracea) oxidized [(14)C]choline to betainal and betaine, as did protoplast lysates. Upon differential centrifugation, the [(14)C]choline-oxidizing activity of lysates sedimented with chloroplasts. Chloroplasts purified from protoplast lysates by a Percoll cushion procedure retained strong [(14)C]choline-oxidizing activity (1-3 nmol/mg of chlorophyll per hr), although the proportion of the intermediate, [(14)C]betainal, in the reaction products was usually higher than for protoplasts. Isolated chloroplasts also readily oxidized [(14)C]betainal to betaine (20-100 nmol/mg of chlorophyll per hr). Light increased the oxidation of both [(14)C]choline and [(14)C]betainal by isolated chloroplasts approximately 3-fold; this light-stimulation was abolished by 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU). Similar results were obtained with another chenopod (Beta vulgaris) but not with pea (Pisum sativum), a species that accumulates no betaine. The chloroplast site for betaine synthesis in chenopods contrasts with the mitochondrial site in mammals.

Journal Article↗