Analysis of human follistatin structure: identification of two discontinuous N-terminal sequences coding for activin A binding and structural consequences of activin binding to native proteins.

Wang, Q; Keutmann, H T; Schneyer, A L; Sluss, P M

Wang, Q; Keutmann, H T; Schneyer, A L; Sluss, P M.

Affiliation

Wang Q; Reproductive Endocrine Unit, Massachusetts General Hospital, Boston 02114, USA.

Endocrinology ; 141(9): 3183-93, 2000 Sep.

Article in En | MEDLINE | ID: mdl-10965889

Subject(s)

Glycoproteins/genetics; Inhibins/metabolism; Activins; Amino Acid Sequence; Antibodies, Monoclonal; Electrophoresis, Polyacrylamide Gel; Epitopes/genetics; Follistatin; Glycoproteins/biosynthesis; Heparitin Sulfate; Humans; Ligands; Molecular Sequence Data; Molecular Weight; Peptide Mapping; Protein Binding; Protein Conformation; Proteins/chemistry; Proteins/genetics; Sulfhydryl Compounds/chemistry

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Collection: 01-internacional Database: MEDLINE Main subject: Glycoproteins / Inhibins Type of study: Diagnostic_studies / Prognostic_studies Limits: Humans Language: En Journal: Endocrinology Year: 2000 Type: Article Affiliation country: United States

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