Characterization of the type of carbohydrate chains of the higher molecular weight (140 kDa) acid phosphatase of the frog liver

1.1. The higher molecular weight, (HMW, Mr 140 kDa) acid phosphatase (AcPase) of the frog liver (Rana esculenta) was separated into enzymatically active components by isoelectric focusing in an immobilized pH gradient and their carbohydrate chains were analyzed by specific lectin binding after nativ...

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Bibliographic Details
Published inInternational journal of biochemistry Vol. 25; no. 12; pp. 1957 - 1961
Main Authors Kubicz, Aleksandra, Szalewicz, Agata
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 01.12.1993
Pergamon
Subjects
Acid Phosphatase - chemistry
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Carbohydrate Sequence
Carbohydrates - chemistry
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Lectins - metabolism
Liver - enzymology
Molecular Sequence Data
Molecular Weight
Rana esculenta
HRP, horse radish peroxidase
WGA, wheat germ agglutinin
IEF, isoelectrofocusing
LMW, lower molecular weight
PNA, peanut agglutinin
NC, nitrocellulose
IPG-EF, isoelectro-focusing in immobilized pH gradients
ConA, concanavalin A
DAB, diaminobenzidine tetrachloride
HMW, higher molecular weight
AcPase, acid phosphatase
LcH, Lens culinaris hemagglutinin
Binding
Lectin
Enzyme
Liver
Amphibia
Phosphoric monoester hydrolases
Esterases
Salientia
Vertebrata
Blotting assay
Rana esculenta
Hydrolases
Carbohydrate chain
Acid phosphatase
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Summary:1.1. The higher molecular weight, (HMW, Mr 140 kDa) acid phosphatase (AcPase) of the frog liver (Rana esculenta) was separated into enzymatically active components by isoelectric focusing in an immobilized pH gradient and their carbohydrate chains were analyzed by specific lectin binding after native blotting.2.2. The lectin-binding patterns obtained with ConA, WGA, LcH and PNA as well as with WGA and PNA after desialylation indicate that the frog liver HMW AcPase contains predominantly N-linked complex and/or hybride type carbohydrate chains with terminal sialic acid and fucose residues; O-glycosylated enzyme components with free and sialic acid substituted Gal-GalNAc sequences were also detected.
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ISSN:0020-711X
DOI:10.1016/0020-711X(88)90331-X