Purification and characterization of recombinant human activin B

Charles H. Schmelzer; Louis E. Burton; Cathleen M. Tamony; Ralph H. Schwall; Anthony J. Mason; Nanette Liegeois

doi:10.1016/0167-4838(90)90178-I

Purification and characterization of recombinant human activin B

Charles H. Schmelzer, Louis E. Burton, Cathleen M. Tamony, Ralph H. Schwall, Anthony J. Mason, Nanette Liegeois

School of Medicine

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

Recombinant human activin B has been isolated to more than 95% purity from a mammalian kidney cell line. Activin B is a covalently-linked homodimer with an apparent molecular mass of 25.9 kDa (unreduced) and 15.2 kDa (reduced) as determined by SDS-polyacrylamide-gel electrophoresis. On gel filtration in 6 M guanidine hydrochloride, activin B chromatographs with an apparent molecular mass of 11 kDa, whether reduced or not. The amino-terminal sequence of the purified protein is consistent with the expected sequence derived from the β subunit of inhibin B. The amino acid composition of the purified molecule agrees with the expected theoretical composition of the β subunit of inhibin B. Activin B has an apparent pI of 4.6 as determined by isoelectric focusing in 6 M urea and 4.7 as determined by chromatofocusing in 6 M urea. The extinction coefficient is 1.8.

Original language	English (US)
Pages (from-to)	135-141
Number of pages	7
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	1039
Issue number	2
DOIs	https://doi.org/10.1016/0167-4838(90)90178-I
State	Published - Jun 19 1990

Keywords

Activin A
Activin B
Growth factor
Protein purification

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology

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10.1016/0167-4838(90)90178-I

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title = "Purification and characterization of recombinant human activin B",

abstract = "Recombinant human activin B has been isolated to more than 95% purity from a mammalian kidney cell line. Activin B is a covalently-linked homodimer with an apparent molecular mass of 25.9 kDa (unreduced) and 15.2 kDa (reduced) as determined by SDS-polyacrylamide-gel electrophoresis. On gel filtration in 6 M guanidine hydrochloride, activin B chromatographs with an apparent molecular mass of 11 kDa, whether reduced or not. The amino-terminal sequence of the purified protein is consistent with the expected sequence derived from the β subunit of inhibin B. The amino acid composition of the purified molecule agrees with the expected theoretical composition of the β subunit of inhibin B. Activin B has an apparent pI of 4.6 as determined by isoelectric focusing in 6 M urea and 4.7 as determined by chromatofocusing in 6 M urea. The extinction coefficient is 1.8.",

keywords = "Activin A, Activin B, Growth factor, Protein purification",

author = "Schmelzer, {Charles H.} and Burton, {Louis E.} and Tamony, {Cathleen M.} and Schwall, {Ralph H.} and Mason, {Anthony J.} and Nanette Liegeois",

year = "1990",

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T1 - Purification and characterization of recombinant human activin B

AU - Schmelzer, Charles H.

AU - Burton, Louis E.

AU - Tamony, Cathleen M.

AU - Schwall, Ralph H.

AU - Mason, Anthony J.

AU - Liegeois, Nanette

PY - 1990/6/19

Y1 - 1990/6/19

N2 - Recombinant human activin B has been isolated to more than 95% purity from a mammalian kidney cell line. Activin B is a covalently-linked homodimer with an apparent molecular mass of 25.9 kDa (unreduced) and 15.2 kDa (reduced) as determined by SDS-polyacrylamide-gel electrophoresis. On gel filtration in 6 M guanidine hydrochloride, activin B chromatographs with an apparent molecular mass of 11 kDa, whether reduced or not. The amino-terminal sequence of the purified protein is consistent with the expected sequence derived from the β subunit of inhibin B. The amino acid composition of the purified molecule agrees with the expected theoretical composition of the β subunit of inhibin B. Activin B has an apparent pI of 4.6 as determined by isoelectric focusing in 6 M urea and 4.7 as determined by chromatofocusing in 6 M urea. The extinction coefficient is 1.8.

AB - Recombinant human activin B has been isolated to more than 95% purity from a mammalian kidney cell line. Activin B is a covalently-linked homodimer with an apparent molecular mass of 25.9 kDa (unreduced) and 15.2 kDa (reduced) as determined by SDS-polyacrylamide-gel electrophoresis. On gel filtration in 6 M guanidine hydrochloride, activin B chromatographs with an apparent molecular mass of 11 kDa, whether reduced or not. The amino-terminal sequence of the purified protein is consistent with the expected sequence derived from the β subunit of inhibin B. The amino acid composition of the purified molecule agrees with the expected theoretical composition of the β subunit of inhibin B. Activin B has an apparent pI of 4.6 as determined by isoelectric focusing in 6 M urea and 4.7 as determined by chromatofocusing in 6 M urea. The extinction coefficient is 1.8.

KW - Activin A

KW - Activin B

KW - Growth factor

KW - Protein purification

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AN - SCOPUS:0025368271

SN - 0167-4838

VL - 1039

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JO - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

JF - Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular

IS - 2

ER -

Purification and characterization of recombinant human activin B

Abstract

Keywords

ASJC Scopus subject areas

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