The functional molecular mass of the Pasteurella hyaluronan synthase is a monomer

• Published in: Biochimica et biophysica acta Vol. 1770; no. 2; pp. 286 - 290
• Main Authors: Pummill, Philip E., Kane, Tasha A., Kempner, Ellis S., DeAngelis, Paul L.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2007
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Chromatography, Gel; Cloning, Molecular; Escherichia coli - enzymology; Escherichia coli - genetics; Glucosephosphate Dehydrogenase - metabolism; Glucuronosyltransferase - chemistry; Glucuronosyltransferase - isolation & purification; Glucuronosyltransferase - metabolism; Glucuronosyltransferase - radiation effects; Glycosaminoglycan; Glycosyltransferase; Hyaluronan; Hyaluronan synthase; Hyaluronan Synthases; Molecular Weight; Pasteurella multocida; Pasteurella multocida - enzymology; Radiation inactivation; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; SDS; GT2; Glycosyltransferase; kDa; SEC-MALLS; GAG; Hyaluronan synthase; Radiation inactivation; Tris; Pasteurella multocida; GlcUA; BSA; Hyaluronan; G6P-DH; MALDI-ToF MS; HA; Glycosaminoglycan; GlcNAc; HAS; PCR

Hyaluronan (HA), a linear polysaccharide composed of β1,3-GlcNAc-β1,4-GlcUA repeats, is found in the extracellular matrix of vertebrate tissues as well as the capsule of several pathogenic bacteria. All known HA synthases (HASs) are dual-action glycosyltransferases that catalyze the addition of two...