A re-appraisal of multiplicity of endoglucanase I from Trichoderma reesei using monoclonal antibodies and plasma desorption mass spectrometry.

@article{Luderer1991ARO,
  title={A re-appraisal of multiplicity of endoglucanase I from Trichoderma reesei using monoclonal antibodies and plasma desorption mass spectrometry.},
  author={M E Luderer and Franz Hofer and Klaus D. Hagspiel and G{\"u}nter Allmaier and Dieter Blaas and Christian Peter Kubicek},
  journal={Biochimica et biophysica acta},
  year={1991},
  volume={1076 3},
  pages={427-34}
}
An endo beta-1,4-glucanase (EC 3.2.1.4, 1.4-(1,3;1,4)-beta-D-glucan 4 glucanhydrolase) was purified to apparent homogeneity from culture filtrates of Trichoderma reesei QM 9414. Identity of the protein with endoglucanase I (EG I) was examined by subjecting CNBr fragments of the protein to analysis by plasma desorption mass spectrometry. Seven non-glycosylated fragments, mapped on the eg1 gene sequence, could be identified, hence proving at least 39.4% identity of the amino acid sequence. No… CONTINUE READING