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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 P 1 ‐destroying enzyme as A 1,4‐α‐galactosidase
Author(s) -
Yates A.D.,
Morgan W.T.J.,
Watkins Winifred M.
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80731-9
Subject(s) - enzyme , galactosidases , biochemistry , chemistry , biology , beta galactosidase , escherichia coli , gene
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 isolated from hydatid cyst fluids [2,3 ] and., as PI specificity is dependent on a terminal non-reducing a-galactosyl residue [3,4] , it was inferred that the enzyme concerned was also an a-galactosidase. The isolation of three linkage-specific ol-D-galactosidases from T. foetus extracts is described in this paper. The enzyme that destroys blood-group B specificity is characterised as a 1,3-a+galactosidase, the enzyme that destroys blood-group PI-specificity as a 1,4-cu-galactosidase, and the third enzyme as a 1,6-c+ galactosidase which also hydrolyses alkyl and aryl a-Dgalactosides.