Results 181 to 190 of about 18,264 (210)

Genes encoding polygalacturonases

Plant Molecular Biology Reporter, 1994
(DG) Department of Physiology and Environmental Science, University of Nottingham, Sutton Bonington, Loughborough LE12 5RD, United Kingdom (CB) Jealott's Hill Research Station, Zeneca Seeds, Bracknell, Berkshire, RG12 6EY, UK (DDP) Plant Sciences, University of Arizona, Tucson, AZ 85721, USA (RM) Laboratoire de Biologie Mol6culaire V6g6tale, Universit6
Don Grierson, Colin Bird, Dean DellaPenna, Régie Mache   +3 more
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Inhibition of polygalacturonase from Verticillium dahliae by a polygalacturonase inhibiting protein from cotton

Phytochemistry, 2001
An extracellular endo-polygalacturonase (PGase) [E.C. 3.2.1.15] was isolated from 18-day-old culture filtrates of Verticillium dahliae and partially purified using gel permeation chromatography. The band responsible for PGase activity was electrophoretically characterized as having a molecular mass of approximately 29 500 and an isoelectric point of 5 ...
J T, James, I A, Dubery
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Polygalacturonase activity in starfruit

Food Chemistry, 1987
Abstract Polygalacturonase (PGase) was extracted and partially purified from ripe starfruit (Averrhoa carambola, L.). 2·3- and 7·8-fold purifications were obtained following purification by Amicon ultrafiltration and Sephadex G-100 filtration, respectively.
Ghazali, H.M., Leong, C.K.
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Characterization of polygalacturonases

Gene, 1993
Lei et al. [Gene 117 (1992) 119-124] recently published the nucleotide sequence of the peh gene of Erwinia carotovora subsp. carotovora (Ecc) and a characterization of its product endopolygalacturonase (Peh). The gene appears highly similar to previously described peh sequences of Ecc [Hinton et al., Mol. Microbiol. 4 (1990) 1029-1036; Saarilahti et al.
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Two forms of polygalacturonase in tomatoes

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract Two polygalacturonidases, (poly--1, 4-galacturonide glycanobydrolase, EC 3.2.1.15) (polygalacturonases I and II) have been separated from extracts of ripe tomatoes by chromatography on DEAE-Sephadex A-50. Polygalacturonase II was the predominant enzyme in all of the samples examined.
R, Pressey, J K, Avants
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Polygalacturonase inhibitors in bean pods

Phytochemistry, 1996
The amount of polygalacturonase-inhibiting protein (PGIP) was 14 times higher in bean pods than in etiolated hypocotyls. The PGIP was extracted from bean pods and partially purified by chromatography on columns of S-Sepharose. DEAE-Sephadex A-50, and Sephadex G-75.
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A quantitative bioassay specific for polygalacturonases

Analytical Biochemistry, 1969
Abstract A bioassay for PG activity based on fresh weight loss of cucumber pericarp tissue is described which is specific, quantitative, sensitive and reproducible. The assay is at least 500 times more sensitive than previously described techniques.
H W, Mussell, D J, Morre
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Molecular Evolution of Fungal Polygalacturonase

1986
In plant-fungi interactions the establishment of basic compatibility occurs when a potential pathogen acquires functions that allow colonization of host plant species and/or suppression or neutralization of host resistance responses. Cultivar and race-specific resistance (specific compatibility) is generally considered as superimposed in host-parasite ...
CERVONE, Felice, DE LORENZO, Giulia, SALVI, Giovanni, CAMARDELLA L.   +3 more
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Determination of Polygalacturonase in Fruits

Nature, 1962
THE action of polygalacturonase1 is most commonly investigated either by viscometry2 or by the Willstatter-Schudel hypoiodite procedure3. Recently, Foda4 showed that the enzyme action was more conveniently and rapidly measured by using a colorimetric method based on that of Willaman and Davison5.
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Bean polygalacturonase inhibitor protein-1 (PGIP-1) inhibits polygalacturonases from Stenocarpella maydis

Physiological and Molecular Plant Pathology, 2000
Stenocarpella maydis, a fungal pathogen of maize, produced polygalacturonases (PGs) when grown on pectin or maize cell walls. An extract from bean (Phaseolus vulgaris L.) which contained an active inhibitor of Aspergillus niger PG, also inhibited S. maydis PG in a reducing sugar assay.
D.K Berger, D Oelofse, M.S Arendse, E Du Plessis, I.A Dubery   +4 more
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