Purification, characterization and cDNA cloning of an endo-exonuclease from the basidiomycete fungus Armillaria mellea
نویسندگان
چکیده
منابع مشابه
Purification, characterization and cDNA cloning of an endo-exonuclease from the basidiomycete fungus Armillaria mellea.
We have purified an endo-exonuclease from the fruiting body of the basidiomycete fungus Armillaria mellea by using an ethanol fractionation step, followed by two rounds of column chromatography. The enzyme had an apparent molecular mass of 17500 Da and was shown to exist as a monomer by gel-filtration analysis. The nuclease was active on both double-stranded and single-stranded DNA but not on R...
متن کاملMicrosatellite markers for the diploid basidiomycete fungus Armillaria mellea.
We isolated and characterized 12 microsatellite markers for two North American populations (California, Pennsylvania) of Armillaria mellea, a fungal pathogen responsible for Armillaria root disease of numerous woody plants. Allele frequency ranged from two to nine alleles per locus, and gene diversity ranged from 0.05 to 0.86. Of the 12 loci, eight loci were polymorphic in the California and Pe...
متن کاملAn endo-exonuclease from meiotic tissues of the basidiomycete Coprinus cinereus. Its purification and characterization.
An endo-exonuclease has been identified and partially purified from the basidiocarp tissues of the basidiomycete Coprinus cinereus, which include synchronous meiosis at karyogamy-pachytene stages. Its peak activity appears during the meiotic prophase. The Coprinus endo-exonuclease has a single-strand specific endonuclease activity that converts the supercoiled DNA to relaxed DNA. The endonucleo...
متن کاملPurification and characterization of a mammalian endo-exonuclease.
An endo-exonuclease has been purified from cultured monkey (CV-1) cells. The enzyme which was purified to near homogeneity to be a 65 kDa monomeric protein. The single-strand DNase activity is endonucleolytic and nonprocessive, whereas the double-strand DNase activity is exonucleolytic and processive. The enzyme was also found to have RNase activity using poly-rA as substrate. The pH optimum fo...
متن کاملPurification, characterization, and cDNA cloning of profilin from Phaseolus vulgaris.
Profilin from common bean (Phaseolus vulgaris L.) was purified to homogeneity by poly-L-Pro affinity chromatography and gel filtration. The hypocotyl and symbiotic root nodule protein was detected as a single isoform with a 14.4-kD molecular mass and an isoelectric point of 5.3. Partial amino acid and DNA sequencing of a full-length cDNA clone confirmed its identity as profilin. An antibody gen...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1999
ISSN: 0264-6021
DOI: 10.1042/0264-6021:3390713