Author: "Collada, C." / Subject: cotyledons and chitinase - PubAg Search Results

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1. Basic endochitinases are major proteins in Castanea sativa cotyledons

Author:: Collada, C., et al. ; Casado, R.; Fraile, A.; Aragoncillo, C.; Show all 4 Authors
Source:: Plant physiology 1992 v.100 no.2 pp. 778-783
ISSN:: 0032-0889
Subject:: fungal diseases of plants; antifungal properties; cotyledons; chitinase; amino acid sequences; Castanea sativa; enzyme activity; defense mechanisms
Abstract:: ... Basic endochitinases are abundant proteins in Castanea sativa Mill. cotyledons. Three basic chitinases were purified with molecular masses of 25, 26, and 32 kD (Ch1, Ch2, and Ch3) and with isoelectric points between 8 and 9.5. Antibodies raised against Ch1 cross-reacted with Ch2 and Ch3. However, Ch3 showed differences when compared with the other two enzymes, especially in its higher cysteine con ...
DOI:: 10.1104/pp.100.2.778
PubMed:: 16653058
: http://dx.doi.org/10.1104/pp.100.2.778

2. Endochitinases from Castanea crenata cotyledons

Author:: Collada, C., et al. ; Casado, R.; Aragoncillo, C.; Show all 3 Authors
Source:: Journal of agricultural and food chemistry 1993 v.41 no.10 pp. 1716-1718
ISSN:: 0021-8561
Subject:: Castanea crenata; chitinase; isozymes; molecular weight; enzyme activity; cotyledons; amino acids; amino acid composition
Abstract:: ... Three constitutive endochitinase isoforms were purified from the cotyledons of Castanea crenata. All three isoforms are basic with pI between 8.5 and 9, possess approximate molecular weights of 25 000, 26 000, and 25 500, and have been named Cha, Chb, and Chc, respectively. All isoforms cross-reacted with antibodies raised against Ch1 chitinase previously purified from Castanea sativa. The molecul ...
DOI:: 10.1021/jf00034a037
: http://dx.doi.org/10.1021/jf00034a037