beta-N-acetylhexosaminidases from Serratia marcescens.
Two forms of beta-N-acetylhexosaminidase from Serratia marcescens with an optimum pH of 5.0 and 6.5, respectively, to 4-methylumbelliferyl-2-acetamido-2-deoxy-beta-D-glucopyranoside were separated by DEAE-cellulose chromatography and Sephacryl S-200 chromatography. On the basis of their molecular weights, thermal stability, substrate specificity and isoelectric points, the form with an acidic pH optimum resembled hexosaminidase B, whereas the form with a neutral pH optimum resembled hexosaminidase C. Lectin binding studies showed that the acidic form does not bind to concanavalin-A-Sepharose, Tetragonolobus purpurea-agarose, wheat germ-agglutinin-Sepharose or Ricinus communis-agglutinin-agarose, whereas the neutral form binds to the last two lectin columns.
Cenci
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Dipartimento di Igiene, Università di Perugia, Italy.
Beccari
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T
Caldini
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Bellachioma
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G
Orlacchio
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A
D006596:Hexosaminidases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000378:metabolism; D012706:Serratia marcescens / Q000201:enzymology*
D037102:Lectins; D006596:Hexosaminidases