Mucins porcine submaxillary mucin

Porcine, submaxillary mucin Porcine, submaxillary mucin a-SA-(2— 6), a-Fuc-(l— 2) none 50... 

T. K. Dam, T. A. Gerken, B. S. Cavada, K. S. Nascimento, T. R. Moura, and C. F. Brewer, Binding studies of a-GalNAc specific lectins to the a-GalNAc (Tn-antigen) form of porcine submaxillary mucin and its smaller fragments, J. Biol. Chem., 282 (2007) 28256-28263. 

A. E. Eckhardt, C. S. Timpte, A. W. DeLuca, and R. L. Hill, The complete cDNA sequence and structural polymorphism of the polypeptide chain of porcine submaxillary mucin, J. Biol. Chem., 272 (1997) 33204—33210. 

T. A. Gerken and N. Jentoft, Structure and dynamics of porcine submaxillary mucin as determined by natural abundance carbon-13 NMR spectroscopy, Biochemistry, 26 (1987) 4689-4699. 

T. A. Gerken, C. L. Owens, and M. Pasumarthy, Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide, J. Biol. Chem., 272 (1997) 9709-9719. 

Porcine submaxillary mucins (100) Porcine (100) and bovine (101) submaxillary mucins... 

Rat, small-intestinal mucosa Porcine, submaxillary mucin o-Fue-(l— 2) none 51... 

Doi M. and See H. Introduction to polymer physics. USA Oxford University Press 1995 Eckhardt A.E., Timpte C.S., Abernethy J.L., Toumadje A., Johnson W.C. and Hill R.L. (1987). Structural properties of porcine submaxillary mucin. J Biol Chem. 262, 11339-11344... 

Perez-Vilar J., Eckhardt, A.E. and Hill R.L. (1996). Porcine submaxillary mucin forms disulfide- b onded dimers between its carboxyl-terminal domains. J Biol Chem. 271, 9845-9850 Perez-Vilar J. and Hill R.L. (1997). Norrie disease protein (norrin) forms disulfide-linked oligomers associated with the extracellular matrix. J Biol Chem 272, 33410-33415 Perez-Vilar J., Eckhardt, A.E., DeLuca A. and Hill R.L. (1998). Porcine submaxillary mucin forms disulfide-linked multimers through its amino-terminal D domains. J Biol Chem. 273, 14442-14449... 

Perez-Vilar J. and Hill R.L. (1998a). The carboxyl-terminal 90 residues of porcine submaxillary mucin are sufficient for forming disulfide-bonded dimers. J Biol Chem 273, 6982-6988 Perez-Vilar J. and Hill R.L. (1998b). Identification of the half-cystine residues in porcine submaxillary mucin critical for multimerization through the D-domains. Roles of the CGLCG motif in the D1 and D3-domains. J Biol Chem 273, 34527-34534 Perez-Vilar J. and Hill R.L. (1999). The structure and assembly of secreted mucins. J Biol Chem 274, 31751-31754... 

In addition to H(O) substances, Matsumoto and Osawa198 reported hemagglutination inhibition by B and A substances and neuraminidase-digested, porcine submaxillary-mucin. Although Lea substance did not inhibit, a closely related milk oligosaccharide, lacto-N-fucopentaose II, did exhibit activity in this assay. On screening 22 invertebrate extracts, Baldo and coworkers found eel-serum-reactive material in 15 species.881... 

Complex, blood-group-active substances have been employed as inhibitors of hemagglutination.196,693 Osawa and Matsumoto found692 inhibition of both Ulex lectins by human A-, B-, and H-active substances, whereas Lea substance and porcine, submaxillary mucin bound only to Ulex II. Chuba and coworkers693 reported that substances from porcine stomach (A-active), equine stomach (B-active), and baboon stomach (A-, B-, and O-active substances), as well as human A-, B-, and O-active substances, bound equally well to both U. europeus lectins. However, porcine, submaxillary mucin and nonsecretor saliva inhibited only Ulex II activity. 

The substrate requirements, linkage specificity, and kinetic mechanism of an q -2,3-sialyltransferase have been compared with an a-2,6-sialyltransferase from porcine submaxillary mucin.The former enzyme will specifically modify glycoproteins and glycolipids which contain 2-acetamido-2-deoxy-3-O S-D-galactosyl-D-galactose sequences. The only acceptor substrates reported for the a-2,6-sialyltransferase are those glycoproteins containing the structure (58). ... 

Figure 4.14 The Biosynthetic Pathways for the Saccharides of Porcine Submaxillary Mucin, as Derived from the Experiments of Beyer et al (1979). For details see the text.

Porcine submaxillary mucin (PSM) was generously supplied by Dr. Pi-Wan Cheng of the Department of Pediatrics, CWRU ([Mresent address Department of Pediatrics, University of North Carolina, Chapel Hill, N.C.), and was prepared by a method similar to that of De Salegui and Plonska but without the hydroxylapatite treatment. The structures of the oligosaccharides of PSM have been determined by Carlson. ... 

Fig. 5. Proposed structures for reduced oligosaccharides isolated from blood group A-positive porcine submaxillary mucin by alkaline borohydride treatment (from Carlson, 1968). Three reduced oligosaccharides are shown in the figure and three others were obtained which are not illustrated above but which were identical to oligosaccharides I, II, and III, respectively, except for the absence of the sialyl residue. Ac, acetyl Gly, glycolyL...

Fig. 12. Biosynthetic pathway for ovine and porcine submaxillary mucins. Prot, protein GalNAc, N-acetyl-n-galactosamine SA, sialic acid Gal, D-galactose OSM, ovine submaxillary mucin PSM, porcine submaxillary mucin. See text for a discussion of this pathway.

Present knowledge on the biosynthesis of the prosthetic groups of OSM and porcine submaxillary mucin (PSM) is summarized in Fig. 12. Five glycosyltransferases are required for the synthesis of the most complex oligosaccharide side chain, the pentasaccharide present in PSM with human blood group A specificity (Carlson, 196, Section II). Four of these five enzymes are required for the synthesis of the side chain of blood group A-negative PSM two transferases are required for incorporation of the disaccharide side chain of OSM. 

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