PMID- 8183285
OWN - NLM
STAT- MEDLINE
DCOM- 19940616
LR  - 20190825
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 31
IP  - 6
DP  - 1994 Apr
TI  - Interaction of hamster submaxillary sialyl-Tn and Tn glycoproteins with Gal, 
      GalNAc and GlcNAc specific lectins.
PG  - 485-90
AB  - Hamster submaxillary glycoprotein (HSM), one of the simplest glycoproteins among 
      mammalian salivary mucins, is composed of approximately equivalent amounts of 
      protein, hexosamine and sialic acid. The Thr and Ser residues in the protein core 
      account for more than half of all of the amino acid residues, while Lys, Glu, Pro 
      and Ala are the major components of the remaining portion of amino acids. The 
      carbohydrate side chains of this mucous glycoprotein have mainly the 
      NeuAc-GalNAc-(sialyl-Tn) sequence (HSM), and those of the desialylated product 
      (HSM-Tn) are almost exclusively unsubstituted GalNAc residues (Tn determinants). 
      The binding properties of sialyl-Tn (HSM) and asialo-HSM (HSM-Tn) glycoproteins 
      were tested by precipitin assay with Gal, GalNAc and GlcNAc specific lectins. The 
      HSM-Tn completely precipitated Vicia villosa (VVL both B4 and mixture of A and 
      B), Maclura pomifera (MPL), and Artocarpus integrifolia (Jacalin) lectins; less 
      than 2 micrograms of HSM-Tn were required for precipitating 50% of 5.0-6.3 
      micrograms lectin nitrogen added. HSM-Tn also reacted well with Helix pomatia 
      lectin (HPL), Wistaria floribunda lectin (WFL) and Abrus precatorius agglutinin 
      (APA) and precipitated in each case over 81% of the lectin nitrogen added. The 
      reactivity of HSM-Tn with other lectins (Ricinus communis, RCA1; Dolichol 
      biflorus, DBL; Viscum album, ML-I; Arachis hypogaea, PNA, and Triticum vulgaris, 
      WGA) was weak or negligible. The activity of sialyl-Tn (HSM) was more restricted; 
      HSM reacted well with Jacalin, moderately with MPL and VVL-B4, but was inactive 
      or only weakly with the other lectins used. These findings indicate that HSM and 
      its desialylated product (HSM-Tn) are highly useful reagents for the 
      differentiation of Tn and T/Gal specific lectins and for anti-T, Tn and Af 
      monoclonal antibodies.
FAU - Wu, A M
AU  - Wu AM
AD  - Glyco-Immunochemistry Research Lab., Chang-Gung Medical College, Tao-yuan, 
      Taiwan.
FAU - Shen, F
AU  - Shen F
FAU - Herp, A
AU  - Herp A
FAU - Wu, J H
AU  - Wu JH
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Lectins)
RN  - 0 (Mucins)
RN  - 0 (Sialic Acids)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Cricetinae
MH  - Hydrolysis
MH  - Lectins/*metabolism
MH  - Molecular Sequence Data
MH  - Mucins/classification/*metabolism
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids
MH  - Submandibular Gland/*chemistry
EDAT- 1994/04/01 00:00
MHDA- 1994/04/01 00:01
CRDT- 1994/04/01 00:00
PHST- 1994/04/01 00:00 [pubmed]
PHST- 1994/04/01 00:01 [medline]
PHST- 1994/04/01 00:00 [entrez]
AID - 10.1016/0161-5890(94)90067-1 [doi]
PST - ppublish
SO  - Mol Immunol. 1994 Apr;31(6):485-90. doi: 10.1016/0161-5890(94)90067-1.