An improved automated periodate-resorcinol method for the determination of sialic acid

1983 ◽  
Vol 133 (1) ◽  
pp. 233-238 ◽  
Author(s):  
Theodore R. Oegema ◽  
Katherine M. Cooper
Keyword(s):  
Sialic Acid ◽  
Resorcinol Method

Automated Method for Determination of Bound N-Acetylneuraminic Acid in Serum

1975 ◽  
Vol 21 (3) ◽  
pp. 412-414 ◽  
Author(s):  
Elisabeth Rey ◽  
Lucile Gerbaut ◽  
Christian Lombart
Keyword(s):  
Sialic Acid ◽  
Present Method ◽  
Acetylneuraminic Acid ◽  
Automated Method ◽  
Resorcinol Method ◽  
Acid Determination

Abstract A modified resorcinol method for sialic acid determination has been successfully adapted to the Technicon AutoAnalyzer. The present method requires only 25 µl of serum, and 30 samples can be analyzed per hour. It may be used to measure sialic acid in concentrations ranging from 10 to 100 mg/liter.

COMPARATIVE ACTION OF VARIOUS OESTROGENIC COMPOUNDS ON MOUSE VAGINAL SIALIC ACIDS (II)

1969 ◽  
Vol 62 (4) ◽  
pp. 663-670 ◽  
Author(s):  
Lars Carlborg
Keyword(s):  
Sialic Acid ◽  
Response Curve ◽  
Sialic Acids ◽  
Clear Cut ◽  
Suitable Parameter ◽  
Sufficient Degree ◽  
Comparative Action ◽  
Relative Potencies ◽  
Good Agreement

ABSTRACT Oestrogens administered in lower doses than necessary to induce full cornification of the mouse vagina induce mucification. It was shown previously that the degree of mucification could be estimated by quantitative determination of sialic acids. A suitable parameter for oestrogen assay was the measurement of vaginal sialic acid concentration which exhibited a clear cut dose response curve. Eleven assays of various oestrogens were performed with this method. Their estimated relative potencies were in good agreement with other routine oestrogen assays. A statistically sufficient degree of precision was found. The sensitivity was of the same order, or slightly higher, than the Allen-Doisy test.

scholarly journals Antiviral adhesion molecular mechanisms for influenza: W. G. Laver's lifetime obsession

2015 ◽  
Vol 370 (1661) ◽  
pp. 20140034 ◽  
Author(s):  
Elspeth F. Garman
Keyword(s):  
Sialic Acid ◽  
Host Cell ◽  
Molecular Mechanisms ◽  
Surface Protein ◽  
X Ray Crystallography ◽  
Sialic Acid Receptors ◽  
Sialic Acid Binding ◽  
Viral Surface Protein ◽  
Viral Surface

Infection by the influenza virus depends firstly on cell adhesion via the sialic-acid-binding viral surface protein, haemagglutinin, and secondly on the successful escape of progeny viruses from the host cell to enable the virus to spread to other cells. To achieve the latter, influenza uses another glycoprotein, the enzyme neuraminidase (NA), to cleave the sialic acid receptors from the surface of the original host cell. This paper traces the development of anti-influenza drugs, from the initial suggestion by MacFarlane Burnet in 1948 that an effective ‘competitive poison’ of the virus' NA might be useful in controlling infection by the virus, through to the determination of the structure of NA by X-ray crystallography and the realization of Burnet's idea with the design of NA inhibitors. A focus is the contribution of the late William Graeme Laver, FRS, to this research.

A Modified Semi-automated Resorcinol Method for the Determination of Inulin

1969 ◽  
Vol 15 (11) ◽  
pp. 1072-1078 ◽  
Author(s):  
Thomas H Steele
Keyword(s):  
Present Method ◽  
Protein Precipitation ◽  
Accuracy And Precision ◽  
Precipitation Procedure ◽  
High Degree ◽  
Automated Methods ◽  
Resorcinol Method ◽  
Urine Specimens

Abstract A semi-automated resorcinol method for the determination of inulin in plasma and urine specimens, using standard AutoAnalyzer modules, is described. Plasma and other protein-containing fluids undergo a preliminary manual protein precipitation procedure. The deproteinized specimens are processed at a rate of 50/hr, with a high degree of accuracy and precision. The superiority of the present method is largely due to the elimination of small acid-resistant pump tubes from the manifold. This is possible because reagents are premixed prior to aspiration into the system, allowing simplification of manifold design over other automated methods.

scholarly journals Nephelometric determination of carbohydrate deficient transferrin

1996 ◽  
Vol 42 (4) ◽  
pp. 551-557 ◽  
Author(s):  
F Schellenberg ◽  
M Martin ◽  
E Cacès ◽  
J Y Bénard ◽  
J Weill
Keyword(s):  
Sialic Acid ◽  
Characteristic Curve ◽  
Anion Exchange Chromatography ◽  
Receiver Operator Characteristic Curve ◽  
Exchange Chromatography ◽  
Treatment Center ◽  
Serum Transferrin ◽  
Receiver Operator Characteristic ◽  
Carbohydrate Deficient Transferrin

Abstract We describe a technique for measuring carbohydrate-deficient transferrin (CDT) in serum. Serum transferrin fractions are separated by anion-exchange chromatography on microcolumns. Sialic acid-deficient transferrin fractions are collected in the eluate, and transferrin is then quantified by a rate-nephelometric technique. Imprecision (CV) was 4-5% within-run and 7-9% between runs (n = 15). Comparison with an isoelectric focusing-immunofixation method for transferrin index (x) yielded y = 761x + 7, Sy/x = 39 mg/L. Assay of sera from 90 abstainers or moderate consumers of alcohol showed that 81 (90%) had CDT concentrations between 30 and 70 mg/L. Among 74 alcoholics admitted to an alcohol treatment center, 54 (73%) had CDT > 70 mg/L, i.e., the diagnostic sensitivity was 73% at a specificity of 90% (area under receiver-operator characteristic curve = 0.891).

Studies on the site of addition of sialic acid and glucosamine to rat α1-acid glycoprotein

1977 ◽  
Vol 55 (4) ◽  
pp. 408-414 ◽  
Author(s):  
J. C. Jamieson
Keyword(s):  
Endoplasmic Reticulum ◽  
Sialic Acid ◽  
Rat Liver ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Main Site ◽  
Acid Glycoprotein ◽  
Membrane Bound ◽  
Polypeptide Chains

Ultrasonic extracts of rough and smooth endoplasmic reticulum fractions and Golgi fractions from rat liver were examined by immunoelectrophoresis using antiserum to α1-acid glycoprotein. Rough endoplasmic reticulum fractions contained only sialic acid free α1-acid glycoprotein, whereas smooth endoplasmic reticulum and Golgi fractions also contained sialic acid containing α1-acid glycoprotein. Determination of the sialic acid contents of immune precipitates isolated from the extracts suggested that the Golgi complex was the main site of addition of sialic acid to α1-acid glycoprotein. Immunological studies on puromycin extracts of polyribosomes showed that polypeptide chains of α1-acid glycoprotein and albumin were assembled mainly on membrane-bound polyribosomes. Evidence is presented from incorporation studies with labelled leucine and glucosamine that initial glycosylation of α1-acid glycoprotein occurs mainly or entirely after release of nascent polypeptide from the ribosomal site.

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