Isolation and Characterization of the K5-Type Yeast Killer Protein and Its Homology with an Exo-β-1,3-glucanase | Zendy

Fatih İzgü | Zendy; Demet Altınbay | Zendy

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Isolation and Characterization of the K5-Type Yeast Killer Protein and Its Homology with an Exo-β-1,3-glucanase

Author(s) -

Fatih İzgü,

Demet Altınbay

Publication year - 2004

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.68.685

Subject(s) - isoelectric point , isoelectric focusing , size exclusion chromatography , yeast , glucanase , chromatography , molecular mass , amino acid , pichia , biology , biochemistry , acetic acid , enzyme , chemistry , ion chromatography , microbiology and biotechnology , recombinant dna , gene , pichia pastoris

K5-type yeast killer protein in the culture supernatant of Pichia anomala NCYC 434 cells was concentrated by ultrafiltration and purified to homogeneity by ion-exchange chromatography with a POROS HQ/M column followed by gel filtration with a TSK G2000SW column. The protein migrated as a single band on discontinuous gradient SDS-PAGE and had a molecular mass of 49,000 Da. The pI value of the K5-type killer protein was measured at pH 3.7 by high voltage vertical gel electrofocusing. The result of an enzyme immuno assay revealed that it was a glycosylated protein. Its internal amino acid sequencing yielded the sequences LNDFWQQGYHNL, IPIGYWAFQLLDNDPY, and YGGSDYGDVVIGIELL, which are 100% identical to exo-beta-1,3-glucanase (accession no. AJ222862) of Pichia anomala (strain K). The purified protein was highly stable at pH values between 3 and 5.5 and temperatures up to 37 degrees C.

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