scholarly journals The sialic acid content and isoelectric point of human kininogen

1975 ◽  
Vol 145 (2) ◽  
pp. 401-403 ◽  
Author(s):  
J C Londesborough ◽  
U Hamberg
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Amino Acid ◽  
Isoelectric Point ◽  
Acid Content ◽  
Low Molecular Weight ◽  
Sialic Acid Content

The sialic acid content of highly purified human kininogen was found to be about 8.6 mol/mol(mol.wt. 50,000). The isoelectric point (pH 4.9 +/- 0.2) is much higher than that of bovine low-molecular-weight kininogen, but is close to that expected from the amino acid and sialic acid analyses.

THE EFFECTS OF SIALIDASE ON PSEUDOCHOLINESTERASE TYPES

1963 ◽  
Vol 41 (1) ◽  
pp. 969-974 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Human Serum ◽  
Acid Content ◽  
Protein Molecule ◽  
Serum Cholinesterase ◽  
Kinetic Properties ◽  
Sialic Acid Content ◽  
Starch Gel ◽  
A Charge

Hereditary variants of human serum cholinesterase were exposed to the action of sialidase. The removal of the sialic acid residues had no effect on the kinetic properties of the esterases but greatly affected the electrophoretic mobility. In starch gel, there were no differences between the pseudocholinesterase types whether sialidase-treated or untreated. This observation permits two conclusions: first, the differences between the esterase types must reside in the protein cores, and second, the different variants must possess equal amounts of sialic acid per protein molecule. According to Liddell et al. there is a charge difference between esterase molecules of different type; since this cannot be accounted for by sialic acid content, the distinguishing characteristics are likely due to differences of amino acid composition.

THE EFFECTS OF SIALIDASE ON PSEUDOCHOLINESTERASE TYPES

1963 ◽  
Vol 41 (4) ◽  
pp. 969-974 ◽  
Author(s):  
D. J. Ecobichon ◽  
W. Kalow
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Human Serum ◽  
Acid Content ◽  
Protein Molecule ◽  
Serum Cholinesterase ◽  
Kinetic Properties ◽  
Sialic Acid Content ◽  
Starch Gel ◽  
A Charge

Hereditary variants of human serum cholinesterase were exposed to the action of sialidase. The removal of the sialic acid residues had no effect on the kinetic properties of the esterases but greatly affected the electrophoretic mobility. In starch gel, there were no differences between the pseudocholinesterase types whether sialidase-treated or untreated. This observation permits two conclusions: first, the differences between the esterase types must reside in the protein cores, and second, the different variants must possess equal amounts of sialic acid per protein molecule. According to Liddell et al. there is a charge difference between esterase molecules of different type; since this cannot be accounted for by sialic acid content, the distinguishing characteristics are likely due to differences of amino acid composition.

scholarly journals The isolation of ovomucoid variants differing in carbohydrate composition

1971 ◽  
Vol 123 (3) ◽  
pp. 399-405 ◽  
Author(s):  
J. G. Beeley
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Acid Content ◽  
Deae Cellulose ◽  
Structure And Function ◽  
Inhibiting Activity ◽  
Carbohydrate Composition ◽  
Charge Heterogeneity ◽  
Sialic Acid Content ◽  
And Function

Three major and two minor species of ovomucoid were separated by chromatography on sulphoethyl-Sephadex. The predominant sialic acid-free species was further resolved into three fractions by DEAE-cellulose chromatography. Although all species of ovomucoid had closely similar trypsin-inhibiting activity, immunochemical properties and amino acid composition, they differ in carbohydrate composition. Wide variation was observed in the content of galactose, N-acetylglucosamine and sialic acid. Charge heterogeneity was related, in part, to variation in sialic acid content. The implications of variable carbohydrate composition for the structure and function of ovomucoid are discussed.

scholarly journals The Effect of Age on the Glycosylation of Human Alpha-2-Macroglobulin

Blood ◽  
2014 ◽  
Vol 124 (21) ◽  
pp. 2800-2800
Author(s):  
Laura S.E. Calvert ◽  
Helen M. Atkinson ◽  
Leslie R. Berry ◽  
Anthony K.C. Chan
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Western Blotting ◽  
Acid Content ◽  
Gel Electrophoresis ◽  
Ricinus Communis ◽  
Apparent Molecular Weight ◽  
Plasma Samples ◽  
Sialic Acid Content ◽  
Sds Page

Abstract Introduction: Alpha-2-macroglobulin (a2m) is a plasma glycoprotein capable of inhibiting all classes of serine proteases. Within the coagulation and fibrinolytic systems, a2m inhibits several critical factors, including thrombin, plasmin, and activated protein C. Previous studies have shown that coagulation factor concentrations are highly variable with age. Notably, a2m levels are approximately twice as high in newborns compared to adults. Elevated levels of a2m in newborns may, in part, contribute to a resistance towards thrombotic events observed in this population. Protein glycosylation is known to affect protein activity as well as pharmacodynamics. The glycosylation profile of adult a2m has previously been analyzed and shown to contain 8 potential sites of N-linked glycosylation. Information regarding glycosylation of a2m in other age groups has yet to be elucidated. Therefore, the purpose of this study is to examine the differences in the glycosylation profiles between newborn and adult a2m. Methods: Normal adult pooled platelet-poor plasma was obtained commercially. Newborn platelet-poor plasma was isolated by standard methods from umbilical cord blood obtained immediately after delivery of healthy full-term infants. Pooled newborn plasma was constructed from 30 different donors. To evaluate the degree of N-linked glycosylation, plasma samples were enzymatically deglycosylated by peptide N-glycosidase F (PNGaseF). Samples were subjected to SDS polyacrylamide (5%) gel electrophoresis (SDS PAGE) and western blotting to detect a2m in plasma. To evaluate a2m sialic acid content, plasma samples were incubated with Neuraminidase from Clostridium perfringens. Following incubation, samples were subjected to native polyacrylamide (4%) gel electrophoresis and western blotting. To detect the presence of non-sialylated terminal galactose residues, plasma samples were incubated with immobilized Ricinus communis lectin, and lectin-bound molecules were separated from unbound molecules by centrifugation. Bound and unbound fractions were subjected to SDS-PAGE and western blotting as described above to detect a2m. Results: Deglycosylation of both newborn and adult a2m with PNGaseF resulted in a change in migration and apparent molecular weight on SDS-PAGE. There was no significant difference (p=0.28, n=3) between the change in apparent molecular weight for newborn a2m (16.1 ± 0.42 kDa) versus adult a2m (14.5 ± 0.99 kDa). On native polyacrylamide gel electrophoresis, newborn a2m exhibited slightly increased migration compared to adult a2m. This difference in migration was abolished following treatment with neuraminidase, indicating the variation in migration was due to differing sialic acid content. Additionally, a lower proportion of newborn a2m was bound to Ricinus communis compared to adult a2m. This indicates newborn a2m has fewer non-sialylated galactose residues available for binding to this lectin. Conclusions: To our knowledge, this is the first study investigating potential glycan heterogeneity between newborn and adult a2m molecules. The results from PNGaseF analyses indicate that there is no macroheterogeneity in total N-glycan content apparent between newborn and adult a2m. However, the observed increase in sialic acid content of newborn a2m compared to adult a2m may be responsible for age-related differences in pharmacodynamic and pharmacokinetic properties of this important protease inhibitor. Disclosures No relevant conflicts of interest to declare.

129: Sialic Acid Content of Urinary TAMM-Horsfall Protein is Reduced in Interstitial Cystitis Patients

2007 ◽  
Vol 177 (4S) ◽  
pp. 44-45
Author(s):  
C. Lowell Parsons ◽  
Mahadevan Rajasekaran ◽  
Marianne Chenoweth ◽  
Paul Stein
Keyword(s):  
Sialic Acid ◽  
Interstitial Cystitis ◽  
Acid Content ◽  
Sialic Acid Content

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

scholarly journals Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1

1988 ◽  
Vol 15 (2) ◽  
pp. 81-84 ◽  
Author(s):  
E. M. Ahmed ◽  
J. A. Applewhite
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Arachis Hypogaea ◽  
Trypsin Inhibitor ◽  
Low Molecular Weight ◽  
Arachis Hypogaea L ◽  
Amino Acid Profiles ◽  
Low Levels

Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

scholarly journals Differences in Sialic Acid Content of Human Interferons

1978 ◽  
Vol 41 (1) ◽  
pp. 175-178 ◽  
Author(s):  
J. Morser ◽  
J. P. Kabayo ◽  
D. W. Hutchinson
Keyword(s):  
Sialic Acid ◽  
Acid Content ◽  
Sialic Acid Content
Sign in / Sign up

Export Citation Format

Share Document