N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans

Reduced Activity

This work investigated the substrate specificity of hNEU enzymes for a glycoprotein substrate (bovine submaxillary mucin) containing 9-<i>O</i>-acetylated and Neu5Gc residues. Using this model substrate, we observe a general trend for hNEU tolerance of Neu5Ac>Neu5Gc>>>Neu5,9Ac<sub>2</sub>, consistent with our previous results with glycolipid substrates. These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity.

Comparison of Procedures for the Isolation of Bovine Submaxillary Mucin

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)64050-5 ◽

1961 ◽

Vol 236 (8) ◽

pp. 2172-2178 ◽

Cited By ~ 8

Author(s):

Shigeru Tsuiki ◽

Yohichi Hashimoto ◽

Ward Pigman

Keyword(s):

Characterisation by mass spectrometry and 1H-NMR of novel hexasaccharides among the acidic O-linked carbohydrate chains of bovine submaxillary mucin

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1992.tb17132.x ◽

1992 ◽

Vol 207 (3) ◽

pp. 973-980 ◽

Cited By ~ 22

Author(s):

Wengang CHAI ◽

Elizabeth F. HOUNSELL ◽

Geoffrey C. CASHMORE ◽

Jerzy R. ROSANKIEWICZ ◽

James FEENEY ◽

...

Keyword(s):

Mass Spectrometry ◽

1H Nmr ◽

Carbohydrate Chains

ACTION OF PROTEOLYTIC ENZYMES ON PURIFIED BOVINE SUBMAXILLARY MUCIN*

Annals of the New York Academy of Sciences ◽

10.1111/j.1749-6632.1963.tb16641.x ◽

2008 ◽

Vol 106 (2) ◽

pp. 233-246 ◽

Cited By ~ 58

Author(s):

Y. Hashimoto ◽

Shigeru Tsuiki ◽

K. Nisizawa ◽

Ward Pigman

Keyword(s):

Proteolytic Enzymes ◽

The Biosynthesis of Bovine Submaxillary Mucin

Studies of Rheumatoid Disease ◽

10.3138/9781442631649-030 ◽

1966 ◽

pp. 259-267

Author(s):

G. Ross Lawford ◽

Harry Schachter

Keyword(s):

Stable thiobarbituric acid chromophore with dimethyl sulphoxide. Application to sialic acid assay in analytical de-O-acetylation

Biochemical Journal ◽

10.1042/bj1590457 ◽

1976 ◽

Vol 159 (3) ◽

pp. 457-462 ◽

Cited By ~ 196

Author(s):

L Skoza ◽

S Mohos

Keyword(s):

Sialic Acid ◽

Homogeneous Solution ◽

Thiobarbituric Acid ◽

Alkaline Treatment ◽

Dimethyl Sulphoxide ◽

Optimal Conditions ◽

Test Mixture ◽

Acetylneuraminic Acid ◽

Thiobarbituric Acid Assay ◽

With dimethyl sulphoxide instead of butanol in the thiobarbituric acid assay for sialic acid, a non-fading chromophore with lambdamax. = 549 nm was produced in a homogeneous solution, allowing dilution of the test mixture in case of high colour yield. This test adapted well to studies on alkaline de-O-acetylation. Bovine and rat submaxillary mucins, and rabbit Tamm-Horsfall urinary sialoproteins contain O-acetyl isomers of neuramine acid that are resistant to the thiobarbituric acid assay. Alkaline de-O-acetylation converted resistant O-acetylneuraminic acid into thiobarbituric acid-reactive sialic acid, and such conversion paralleled de-O-acetylation as measured by the ferric hydroxamate method. The colour increment was similar when the alkaline treatment of bovine submaxillary mucin either preceded or followed the acid hydrolysis. Only alkaline preptreatment was effective with rat submaxillary mucin. By selecting optimal conditions for alkaline de-O-acetylation, O-acetyl isomers can be accurately assessed by the thiobarbituric acid assay.

Sequence of a Second Gene Encoding Bovine Submaxillary Mucin: Implication for Mucin Heterogeneity and Cloning

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.1998.9515 ◽

1998 ◽

Vol 251 (2) ◽

pp. 550-556 ◽

Cited By ~ 6

Author(s):

Weiping Jiang ◽

Joseph T. Woitach ◽

Dwijendra Gupta ◽

Veer P. Bhavanandan

Keyword(s):

Gene Encoding ◽

Structural characterization of sialylated tetrasaccharides and pentasaccharides with blood group H and Lex activity isolated from bovine submaxillary mucin

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb19407.x ◽

1990 ◽

Vol 193 (3) ◽

pp. 837-843 ◽

Cited By ~ 15

Author(s):

Angela V. SAVAGE ◽

John J. DONOHUE ◽

Carolien A. M. KOELEMAN ◽

Dirk H. EIJNDEN

Keyword(s):

Blood Group ◽

Structural Characterization ◽

Blood Group H

Structure determination of five sialylated trisaccharides with core types 1, 3 or 5 isolated from bovine submaxillary mucin

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb19244.x ◽

1990 ◽

Vol 192 (2) ◽

pp. 427-432 ◽

Cited By ~ 32

Author(s):

Angela V. SAVAGE ◽

Carmel M. DONOGHUE ◽

Sinead M. D'ARCY ◽

Carolien A. M. KOELEMAN ◽

Dirk H. EIJNDEN

Keyword(s):

Structure Determination ◽

Probing into the Interaction of Nicotine and Bovine Submaxillary Mucin: NMR, Fluorescence, and FTIR Approaches

Journal of Spectroscopy ◽

10.1155/2016/9580136 ◽

2016 ◽

Vol 2016 ◽

pp. 1-9

Author(s):

Xiaoxiang Liao ◽

Dalin Yuan ◽

Jianguo Tang ◽

Hongqin Yang ◽

Bing Liang ◽

...

Keyword(s):

Fluorescence Spectra ◽

Structure And Function ◽

Acidic Environment ◽

Nmr Data ◽

Synchronous Fluorescence Spectra ◽

Oral Environment ◽

Quenching Mechanisms ◽

And Function ◽

The Impact

Nicotine, the important component of cigarette products, may have an impact on the oral environment after inhalation. The research of interaction between nicotine and bovine submaxillary mucin (BSM) contributes to understand the binding mechanism of nicotine and BSM, and the effects of nicotine on the structure and function of the mucin. NMR data demonstrated that the interaction between nicotine and BSM did exist, and it was pyrrolidyl ring of nicotine playing the major role in the binding. The quenching mechanisms of nicotine and BSM in different pH were different: for acidic environment, the quenching was dynamic; while it became static in the alkaline circumstance. Synchronous fluorescence spectra indicated that nicotine had effect on the microenvironment of the Trp rather than Tyr residue. Meanwhile, the impact of nicotine on the conformation of BSM was also confirmed by 3D fluorescence and FTIR spectra.