| Literature DB >> 7741195 |
Y Taniguchi1, A Ono, M Sawatani, M Nanba, K Kohno, M Usui, M Kurimoto, T Matuhasi.
Abstract
In the course of analyzing the partial amino acid sequences of Cry j I, a major allergen of Japanese cedar (Cryptomeria japonica) pollen, we found a peptide fragment which has a significant homology to some pectate lyase isozymes secreted by plant pathogenic bacteria. Therefore, we investigated whether Cry j I has pectate lyase activity. Cry j I reacted with polygalacturonic acid, resulting in the release of unsaturated uronide products. The optimum temperature and pH for the reaction were 60-70 degrees C and pH 10. The enzymatic reaction had an absolute Ca2+ ion requirement. These characteristics were very compatible with the character of the pectate lyase isozymes reported previously. These results clearly show that Cry j I has pectate lyase activity.Entities:
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Year: 1995 PMID: 7741195 DOI: 10.1111/j.1398-9995.1995.tb02489.x
Source DB: PubMed Journal: Allergy ISSN: 0105-4538 Impact factor: 13.146