Untersuchungen zur physiologischen Bedeutung der Neuraminsäure-haltigen Kohlenhydratgruppe von „Intrinsic-Factor“-Mucoiden menschlicher Magenschleimhaut

Faillard, Hans; Pribilla, W

doi:10.1007/bf01882738

Cited by 14 publications

(1 citation statement)

References 24 publications

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“…A qualitative organ specificity of "prostatic" acid phosphatases is therefore unlikely. This finding confirms biochemicd [31] and immunocytochemical studies that indicated the presence of "prostate-specific" acid phosphatases in leukocytes [29,32], renal collecting tubules [lo], or even in pancreatic islet cell carcinoma [33]. With the unique exception of one isoenzyme from kidney @I = 6.0), we found no other organ-specific acid phosphatase isoenzyme .…”

Section: Zymogram Of Prostatic Acid Phosphatasessupporting

confidence: 91%

Cytochemistry and biochemistry of acid phosphatases V: Electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes

Seitz

Aumüller

1985

The Prostate

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Comparison of zymograms of acid phosphatases (orthophosphoric monoester phosphohydrolase, acid optimum, E.C.3.1.3.2) from human prostate, leukocytes, seminal vesicles, and seminal fluid, separated by analytical isoelectric focusing (IEF), resulted in the identification of three individual groups, particularly of the prostate. These groups contain three molecular forms at different molecular weights and activities in varying quantities and combinations. The molecular weights, estimated by SDS gel electrophoresis, were 1) 86,000, 2) 76,000, and 3) 46,000/50,000 (in a doublet) daltons. None of these isoenzymes were restricted to the prostate, but they were present in very high concentrations in the prostate. Compared to the prostate, the seminal vesicles and isolated leukocytes had very closely related zymograms of acid phosphatases. No specific inhibitor has been found that would selectively inhibit one particular isoenzyme without affecting the others. Protein titration and staining activity of IEF gels at different pH values showed that the isoenzymes from all three groups have high hydrolytic activity of orthophosphoric monoesters beyond the acidic pH range of pH 4-5. Incubation of acidic isoforms of acid phosphatases with neuraminidase did not result in the formation of a homogeneous stem molecule. Further analysis of the secretory moiety using the western blotting method showed a binding of peroxidase-conjugated concanavalin A (Con A), indicating that these isoenzymes are glycoproteins. Moreover, isoenzymes extracted from prostate, seminal fluid, and human leukocytes are immunologically identical.

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Section: Zymogram Of Prostatic Acid Phosphatasessupporting

confidence: 91%

Cytochemistry and biochemistry of acid phosphatases V: Electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes

Seitz

Aumüller

1985

The Prostate

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Chemie und Biologie der Acylneuraminsäuren

Schauera

1973

Angew. Chem.

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In Gangliosid-und in vielen Glykoproteinmolekiilen nehmen Acylneuraminsluren eine sowohl raumlich als auch biologisch-funktionell herausragende Stellung ein. Acylneuraminsauren sind N-und zum Teil auch 0-acylierte Derivate der Neuraminsaure, einer Polyhydroxyamino-ketosiiure, welche die Eigenschaften eines Kohlenhydrats besitzt und daher zur glykosidischen Bindung fahig ist. In diesem Fortschrittsbericht wird ein Uberblick uber unsere Kenntnisse von der Chemie und der Biologie der vor allem im Tierreich weit verbreiteten Acylneuraminsauren gegeben.

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Chemistry and Biology of the Acylneuraminic Acids

Schauer

1973

Angew. Chem. Int. Ed. Engl.

100

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Acylneuraminic acids occupy an outstanding position both sterically and with respect to biological functions in gangliosides and in many glycoprotein molecules. Acylneuraminic acids are N-acylated and partly 0-acylated derivatives of neuraminic acid, a polyhydroxyamino keto acid that has the properties of a carbohydrate and is therefore capable of forming a glycoside linkage. The present report provides a survey of our knowledge of the chemistry and biology of the acylneuraminic acids, which occur widely in particular in the animal kingdom.

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Untersuchungen zur physiologischen Bedeutung der Neuraminsäure-haltigen Kohlenhydratgruppe von „Intrinsic-Factor“-Mucoiden menschlicher Magenschleimhaut

Cited by 14 publications

References 24 publications

Cytochemistry and biochemistry of acid phosphatases V: Electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes

Cytochemistry and biochemistry of acid phosphatases V: Electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes

Chemie und Biologie der Acylneuraminsäuren

Chemistry and Biology of the Acylneuraminic Acids

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