Human FSH isoforms: carbohydrate complexity as determinant of in-vitro bioactivity.

doi:10.1016/s0303-7207(00)00453-6

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Article

Human FSH isoforms: carbohydrate complexity as determinant of in-vitro bioactivity.

Molecular and cellular endocrinology - 28 Mar 2001

Creus S, Chaia Z, Pellizzari E H, Cigorraga S B, Ulloa-Aguirre A, Campo S

Abstract excerpt

Differences in sialic acid content of the hormone have been considered the main determinant of FSH polymorphism. The aim of the present study was to investigate the effect of variations in the oligosaccharide structure of the intrapituitary human FSH (hFSH) glycosylation variants on their intrinsic biological activity. FSH charge isoforms obtained after chromatofocusing were further separated by lectin affinity...

Topics

Animals
Carbohydrate Sequence
Chromatography, Affinity
Concanavalin A
Follicle Stimulating Hormone
Genetic Variation
Humans
Lectins
N-Acetylneuraminic Acid
Oligosaccharides
Pituitary Gland
Plant Lectins
Polymorphism, Genetic
Protein Binding
Protein Isoforms
Rats
Wheat Germ Agglutinins

Source

Open in PubMed

Identifiers

PMID: 11306170
DOI: 10.1016/s0303-7207(00)00453-6

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