Results 181 to 190 of about 18,184 (208)

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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Studies on polygalacturonase of certain yeasts

Archives of Biochemistry and Biophysics, 1951
Abstract 1. 1. Among a considerable number of yeast species, representing nearly all yeast genera, only six were found which were capable of causing certain changes in pectin, when grown in its presence. These six cultures could all be identified with Saccharomyces fragilis (and a variety of this species) and its imperfect form Candida ...
B S, LUH, H J, PHAFF
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PectinaseAspergillus sp. polygalacturonase: Multiplicity, divergence, and structural patterns linking fungal, bacterial, and plant polygalacturonases

Journal of Protein Chemistry, 1993
Nine forms of Aspergillus sp. polygalacturonase were purified from a commercial preparation of pectinase Rohament P using chromatographies and chromatofocusing. Individual forms differ in isoelectric point, and at least five differ in structure; whereas molecular masses and enzymatic properties are largely identical.
E, Stratilová, O, Markovic, D, Skrovinová, L, Rexová-Benková, H, Jörnvall   +4 more
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