PMID: 6459Jun 25, 1976

Purification and characterization of an endo-beta-galactosidase produced by Diplococcus pneumoniae.

The Journal of Biological Chemistry
S Takasaki, A Kobata

Abstract

An endo-beta-galactosidase acting on blood group A and B substances was found in the culture fluid of Diplococcus pneumoniae. The enzyme was purified 1000-fold, and its properties were studied in detail. The enzyme preparation, thus obtained, was practically free from various exoglycosidases, endo-beta-N-acetylglucosaminidase and proteases. The enzyme releases trisaccharides from blood group A and B active mucins purified from ovarian cyst fluid. The structures of the trisaccharides liberated from A and B active mucins were elucidated to be GalNAcalpha1 leads to 3(Fucalpha1 leads to 2)Gal and Galalpha1 leads to 3(Fucalpha1 leads to 2)Gal, respectively. The enzyme also hydrolyzes blood group A and B active oligosaccharides composed of type 2 chains, yielding the same products as in the case of ovarian cyst blood group substances. An H active mucin from ovarian cyst fluid, H active oligosaccharides, and A and B active oligosaccharides with type 1 chains were not hydrolyzed by the enzyme. Consequently, the enzyme catalyzes the following reaction, resulting in the degradation of blood type A and B determinants. (see article).

Related Concepts

Blood Group H Type 1 Antigen
Cations, Divalent
Chloromercuribenzoates
Galactosidase
Kinetics
Mercury
Oligosaccharides
Silver
Streptococcus pneumoniae
Structure-Activity Relationship

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