Linkage‐specific α‐D‐galactosidases from Trichomonas foetus: Characterisation of the blood‐group B‐destroying enzyme as A 1,3‐α‐galactosidase and the blood‐group P1‐destroying enzyme as A 1,4‐α‐galactosidase

@article{Yates1975LinkagespecificF,
  title={Linkage‐specific α‐D‐galactosidases from Trichomonas foetus: Characterisation of the blood‐group B‐destroying enzyme as A 1,3‐α‐galactosidase and the blood‐group P1‐destroying enzyme as A 1,4‐α‐galactosidase},
  author={A. D. Yates and W. Morgan and W. Watkins},
  journal={FEBS Letters},
  year={1975},
  volume={60}
}
Earlier investigations on glycosidases in extracts of the protozoan Trichomonas fbetus indicated that there were at least two distinct ol-D-galactosidases [ 11 ; one acted on low-molecular-weight substrates and differed in heat stability and inhibitory properties from a second enzyme that released a-linked galactose from blood-group B-active structures in glycoproteins. Subsequently the T. foetus extract was found to contain an enzyme that destroyed the blood-group PI activity of a glycoprotein… Expand
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