One of two subunits of masking protein in latent TGF-beta is a part of pro-TGF-beta.
A high molecular mass latent form of transforming growth factor type-beta (TGF-beta) was purified to homogeneity from rat platelets by a seven-step procedure involving group-specific affinity chromatographies on Red-Toyopearl and zinc chelating-Sepharose. The purified latent TGF-beta was a complex of TGF-beta (25 kDa) and the binding protein previously named masking protein (approximately 400 kDa) [(1986) Biochem. Biophys. Res. Commun. 141, 176-184]. Analysis of the peptide structure by gel electrophoresis showed that the masking protein consisted of two subunits of 39 kDa and 105-120 kDa linked by disulfide bonds. N-terminal amino-acid sequencing of the 39 kDa subunit indicated that this subunit was identical to the N-terminal part of the TGF-beta precursor.
Okada
F
F
Tokyo Research Laboratories, Kyowa Hakko Co. Ltd, Japan.
Yamaguchi
K
K
Ichihara
A
A
Nakamura
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001792:Blood Platelets / Q000378:metabolism; D002352:Carrier Proteins / Q000302:isolation & purification*; D053779:Latent TGF-beta Binding Proteins; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011498:Protein Precursors / Q000378:metabolism*; D051381:Rats; D016212:Transforming Growth Factor beta; D015291:Transforming Growth Factors / Q000037:antagonists & inhibitors* / Q000096:biosynthesis / Q000302:isolation & purification
D002352:Carrier Proteins; D053779:Latent TGF-beta Binding Proteins; D046911:Macromolecular Substances; D011498:Protein Precursors; D016212:Transforming Growth Factor beta; D015291:Transforming Growth Factors