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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
13
|
| pubmed:dateCreated |
1988-6-6
|
| pubmed:abstractText |
Human transforming growth factor beta 1 (TGF-beta 1) was purified as a latent high Mr complex from human platelets by a six-step procedure. Analysis by sodium dodecyl sulfate (SDS)-gel electrophoresis under reducing conditions revealed that the complex was composed of at least three components with apparent Mr values of 13,000, 40,000, and 125,000-160,000. The 13-kDa subunit was part of a disulfide-bonded dimer and was identified by amino acid sequencing as TGF-beta 1. The 40-kDa subunit was identified as the amino-terminal part of the TGF-beta 1 precursor lacking the hydrophobic signal sequence. Partial sequencing of the 125-160-kDa protein revealed that it is distinct from known proteins. The 40-kDa and the 125-160-kDa subunits are linked by disulfide bonds, forming a complex with an apparent Mr of 210,000 on SDS gels under nonreducing conditions. Experiments with partial reduction revealed that each complex contains two 40-kDa components linked by disulfide bonds; in addition, the dimer is disulfide-linked to one 125-160-kDa binding protein. TGF-beta 1 binds noncovalently to the 210-kDa complex, and in bound form, TGF-beta 1 is inactive. Incubations of the latent form of TGF-beta 1 at extreme pH values, in 0.02% SDS or in 8 M urea, lead to activation of TGF-beta 1, whereas the complex was resistant to treatment with 5 M NaCl or heat (3 min at 95 degrees C).
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
263
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6407-15
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:3162913-Amino Acid Sequence,
pubmed-meshheading:3162913-Blood Platelets,
pubmed-meshheading:3162913-Chromatography, Gel,
pubmed-meshheading:3162913-Glycosylation,
pubmed-meshheading:3162913-Humans,
pubmed-meshheading:3162913-Hydrogen-Ion Concentration,
pubmed-meshheading:3162913-Molecular Sequence Data,
pubmed-meshheading:3162913-Molecular Weight,
pubmed-meshheading:3162913-Peptides,
pubmed-meshheading:3162913-Transforming Growth Factors
|
| pubmed:year |
1988
|
| pubmed:articleTitle |
Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization.
|
| pubmed:affiliation |
Ludwig Institute for Cancer Research, Uppsala, Sweden.
|
| pubmed:publicationType |
Journal Article
|