Precipitin Reaction between Sd^a-Active Human Tamm-
Horsfall Glycoprotein and Anti-Sd^a Serum

Serafini‐Cessi, Franca; Conte, Roberto

doi:10.1159/000460865

Cited by 3 publications

(2 citation statements)

References 7 publications

(12 reference statements)

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“…and A.S.) were kindly provided by Dr. W. M. Watkins, Clinical Research Centre, Harrow, Middx., U.K. The Sda activity of T-H glycoproteins was measured as detailed by Serafini-Cessi & Conte (1982) and was the minimum concentration (,ug/ml) giving complete inhibition of Sd(a+) red cells induced by human anti-Sda serum. Other glycoproteins were purchased from Sigma.…”

Section: Preparation Ofglycoprotein Acceptorsmentioning

confidence: 99%

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Serafini‐Cessi¹,

Dall’Olio²

1983

Biochemical Journal

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A beta-N-acetylgalactosaminyltransferase that preferentially transferred N-acetylgalactosamine to Sd(a-) Tamm-Horsfall glycoprotein was found in guinea-pig kidney microsomal preparations. This enzyme was kidney-specific and was able to transfer the sugar to other glycoproteins, such as fetuin and alpha 1-acidic glycoprotein. The presence of sialic acid in the acceptors was essential for the transferase activity when either glycoproteins or their Pronase glycopeptides were used as acceptors. Two glycopeptides (Tamm-Horsfall glycopeptides I and II) with a different carbohydrate composition were separated by DEAE-Sephacel chromatography from Pronase-digested Tamm-Horsfall glycoprotein. The amount of N-acetylgalactosamine transferred to glycopeptides by the enzyme correlated with their degree of sialylation. Enzymic digestion of N-[14C]acetylgalactosamine-labelled Tamm-Horsfall glycopeptide II showed that the transferred sugar was susceptible to beta-N-hexosaminidase. The amount of sugar cleaved by beta-hexosaminidase was strongly increased when the labelled Tamm-Horsfall glycopeptide II was pretreated with mild acid hydrolysis, a procedure that removed the sialic acid residues. Alkaline borohydride treatment of the labelled Tamm-Horsfall glycopeptide II did not release radioactivity, thus indicating that enzymic glycosylation took place at the N-asparagine-linked oligosaccharide units of Tamm-Horsfall glycoprotein.

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Section: Preparation Ofglycoprotein Acceptorsmentioning

confidence: 99%

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Serafini‐Cessi¹,

Dall’Olio²

1983

Biochemical Journal

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“…Ten years later, Soh et al . Sd a -active uromodulin can be precipitated by Dolichos and Helix pomatia lectins and by human anti -Sd a [39,40] . Uromodulin is secreted by the kidney and protects against urinary tract infection (UTI).…”

Section: Frequency and Inheritancementioning

confidence: 99%

Sid Antigen

Daniels

FRCPath²

2013

Human Blood Groups

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Comparison between the erythrocyte and urinary Sd^a antigen distribution in a large number of individuals from Emilia‐Romagna, a region of northern Italy*

Conte

Serafini‐Cessi

1991

Transfusion Medicine

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In this study we found that the frequencies of Sda antigen on erythrocytes and urine of a large number of individuals from Emilia-Romagna (a region of northern Italy) are 0.89 and 0.93, respectively. The hypothesis that the infection by pyelonephritogenic Escherichia coli strains with specific adhesins for the alpha 2,3sialyl-galactosyl structure might operate as selective agents for the high frequency of Sda antigen in distal renal cells is discussed.

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Precipitin Reaction between Sd^a-Active Human Tamm- Horsfall Glycoprotein and Anti-Sd^a Serum

Cited by 3 publications

References 7 publications

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Sid Antigen

Comparison between the erythrocyte and urinary Sd^a antigen distribution in a large number of individuals from Emilia‐Romagna, a region of northern Italy*

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Precipitin Reaction between Sd^a-Active Human Tamm- Horsfall Glycoprotein and Anti-Sd^a Serum

Cited by 3 publications

References 7 publications

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Guinea-pig kidney β-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity

Sid Antigen

Comparison between the erythrocyte and urinary Sda antigen distribution in a large number of individuals from Emilia‐Romagna, a region of northern Italy*

Contact Info

Product

Resources

About

Comparison between the erythrocyte and urinary Sd^a antigen distribution in a large number of individuals from Emilia‐Romagna, a region of northern Italy*