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Biomedical subjects

A W Galston

Publications and source records attributed to A W Galston.

At least 19 recordsLinked to original sources
PubMed1991

On the trail of a new regulatory system in plants. Polyomines as modulators of plant development sponsored by Fundación Juan March, Madrid, Spain, February 4-6, 1991.

Investigations into the physiology and biochemistry of polyamines in plants have virtually exploded in the last decade. While not yet accepted by plant physiologists as plant hormones or even as major regulators of plant growth and development, the polyamines require consideration in such varied fields as cell division, organ differentiation, senescence, and stress. We are sure to see more conferences on this subject in the near future.

Adaptation, Physiological↗
PubMed1985

Prevention of a plant disease by specific inhibition of fungal polyamine biosynthesis.

DL-alpha-Difluoromethylornithine (DFMO), an inhibitor of the polyamine biosynthetic enzyme ornithine decarboxylase (EC 4.1.1.17), strongly retards the growth of several species of phytopathogenic fungi in vitro. Such inhibition can be completely reversed by putrescine or spermidine, confirming the essentiality of polyamines for growth of fungal hyphae. We now show that DFMO can protect bean plants (Phaseolus vulgaris Linnaeus cv. Pinto) against infection by uredospores of the bean rust fungus, Uromyces phaseoli Linnaeus, race O. Unifoliolate leaves of 10-day-old greenhouse-grown seedlings were sprayed with 400 microliter per leaf of DFMO at various concentrations in 0.01% Tween 20 at pH 7.0 before or after inoculation with uredospores of Uromyces. After 16 hr in darkness in dew chambers to facilitate spore germination, plants were transferred to the greenhouse, arranged randomly, and examined for local lesions 7 days later. All concentrations of DFMO 0.50 mM or higher gave complete protection against the pathogen; at lower concentrations, postinoculation treatments with DFMO were generally more effective than preinoculation. The appearance of lesions on plants treated with lower concentrations of DFMO was retarded 2-6 days. DFMO also confers protection on unsprayed parts of treated plants, indicating the translocation of some protective effect from sprayed areas. DL-alpha-Difluoromethylarginine, an analogous inhibitor of arginine decarboxylase (EC 4.1.1.19), which is the rate-limiting enzyme in an alternative pathway for polyamine biosynthesis in higher plants, confers no protection even at 5 mM. This emphasizes ornithine decarboxylase as the biochemical locus of choice for the prevention of plant diseases by inhibiting polyamine metabolism.

Arginine↗
PubMed1974

Potassium flux and leaf movement in Samanea saman. I. Rhythmic movement.

Samanea leaflets usually open in white light and fold together when darkened, but also open and dose with a circadian rhythm during prolonged darkness. Leaflet movement results from differential changes in the turgor and shape of motor cells on opposite sides of the pulvinus; extensor cells expand during opening and shrink during closure, while flexor cells shrink during opening and expand during closure but change shape more than size. Potassium in both open and closed pulvini is about 0.4 N. Flame photometric and electron microprobe analyses reveal that rhythmic and light-regulated postassium flux is the basis for pulvinar turgor movements. Rhythmic potassium flux during darkness in motor cells in the extensor region involves alternating predominance of inwardly directed ion pumps and leakage outward through diffusion channels, each lasting ca 12 h. White light affects the system by activating outwardly directed K(+) pumps in motor cells in the flexor region.

Biological Transport, Active↗
PubMed1974

Potassium flux and leaf movement in Samanea saman. II. Phytochrome controlled movement.

Phytochrome, a membrane-localized biliprotein whose conformation is shifted reversibly by brief red or far-red light treatments, interacts with the rhythmic oscillator to regulate leaflet movement and potassium flux in pulvinal motor cells of Samanea. Darkened pinnae exposed briefly to red light (high P(fr) level) have less potassium in motor cells in the extensor region, more potassium in motor cells in the flexor region, and smaller angles than those exposed to far-red light (low P(fr) level). Increase in temperature from 24 degrees to 37 degrees increases the differential effect of the light treatments during opening (the energetic phase) but not during closure, implying that phytochrome controls an energetic process. It seems likely that phytochrome interacts with rhythmically controlled potassium pumps in flexor and extensor cells. During nyctinastic closure of white-illuminated pinnae, exposure to far-red light before darkening results in larger angles than does exposure to red. As in rhythmic opening, the angles of all pinnae and the differential effect of the light treatments increases with increasing temperature.

Bile Pigments↗
PubMed1973

Protein synthesis during endogenous rhythmic leaflet movement in Albizzia.

A rhythm was found in protein synthesis accompanying rhythmic leaflet opening and closing in the dark in the plant Albizzia. More protein was synthesized during the opening of the leaflets than during the closing. Furthermore, an inhibitor of protein synthesis, cycloheximide, prevented rhythmic opening of leaflets but had no effect on rhythmic closing. It is suggested that protein synthesis is involved in the movement across membranes of K(+) ions that cause turgor changes and leaflet movement.

Circadian Rhythm↗
PubMed1970

Herbicide usage.

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Abnormalities, Drug-Induced↗
PubMed1970

Localization of adenosine triphosphatase activity on the chloroplast envelope in tendrils of Pisum sativum.

When samples of pea tendril tissue were incubated in the Wachstein-Meisel medium for the demonstration of adenosine triphosphatases, deposits of lead reaction product were localized between the membranes of the chloroplast envelope. The presence of Mg(2+) was necessary for adenosine triphosphatase activity, and Ca(2+) could not substitute for this requirement. Varying the pH of incubation to 5.5 or 9.4 inhibited enzyme activity, as did the addition of p-chloromercuribenzoic acid or N-ethylmaleimide. The adenosine triphosphatase was apparently inactivated or degraded when the plants were grown in the dark for 24 hours prior to incubation. The enzyme was substrate-specific for adenosine triphosphate; no reaction was obtained with adenosine diphosphate, uridine triphosphate, inosine triphosphate, p-nitrophenyl phosphate, and sodium beta-glycerophosphate. Sites of nonspecific depositions of lead are described. The adenosine triphosphatase on the chloroplast envelope may be involved in the light-induced contraction of this organelle.

Adenosine Triphosphatases↗
PubMed1970

Ontogeny and hormonal control of polyphenoloxidase isozymes in tobacco pith.

Isozymes of tobacco pith polyphenoloxidases (o-diphenol oxidase, EC 1.10.3.1) were separated electrophoretically from fresh pith of intact plants and from cultured pith sections. Extracts of fresh pith contained a poorly resolved complex of two to three anodic bands after starch gel electrophoresis at alkaline pH. This anodic complex was more active with chlorogenic acid than with 3,4-dihydroxyphenylalanine and was found in greater activity per gram fresh weight of tissue in younger internodes than in older ones. The longitudinal gradient of activity was thus the opposite of that found for the constitutive isozymes of peroxidase.A well defined cathodic band of polyphenoloxidase activity appeared after culture of pith in modified White's medium with shaking. This band, which was more active with 3,4-dihydroxyphenylalanine than with chlorogenic acid, could be detected after 1 to 2 days of incubation. Its appearance was enhanced by the addition of 10 mum indoleacetic acid; kinetin (1 mum tended to prevent this indoleacetic acid effect). Such hormonal control is opposite to that previously reported for the rapidly appearing new isozymes of peroxidase. The pattern of the major isozymes associated with polyphenoloxidase activities differs from that of peroxidase.

Catechol Oxidase↗
PubMed1969

Lesser of 2 evils.

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Biodegradation, Environmental↗
PubMed1967

Indoleacetic acid oxidase activity of apoperoxidase.

The conventional activity of electrophoretically purified horseradish peroxidase toward guaiacol, pyrogallol, 2,6-dimethoxyphenol, and benzidine is abolished by removal of the heme prosthetic group with a mixture of cold acetone and hydrogen chloride. The apoenzyme, though devoid of peroxidase activity, retains its activity as an indoleacetic acid oxidase when it is supplied with 10(-5) mole of manganous ion and 2,4-dachlorophenol per liter. This oxidase activity is cyanide-sensitive; azide also inhibits under specific conditions of both pH and cofactor concentration. Partial restoration of the peroxidase activity by recombination of apoprotein with heme produces no effect on the oxidase activity, except that cofactors are no longer absolutely required. Therefore, it appears that the activity of peroxidase as an indoleacetic acid oxidase need not directly involve the heme prosthetic group, or that manganous ions and dichlorophenol can substitute for the heme group in the reaction between indoleacetic acid and oxidase.

Azides↗