Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1978-2-18
pubmed:abstractText
In the stroma-free hemolysate of rabbit reticulocytes there exists a respiratory inhibitor (RF) of protein nature. It could be purified by the following procedure: (NH4)2SO4-precipitation leads to DEAE-Sephadex A-50-chromatography leads to isoelectric focusing leads to gelfiltration on Sephadex G-200. In addition to the activity the identity of the inhibitor could be proved immunologically at all steps of the purification. A molecular weight of about 80,000 was determined by gelelectrophoresis in the SDS-mercaptoethanol-system. The protein has an IP of 5.55--5.65 and consists of one polypeptide chain. This could be shown both by SDS-gelelectrophoresis and by estimation of only one N-terminal amino acid residue (glycine). Only after oxidation with performic acid the amino acid analysis of the protein gives reproducible values. The sum of weight-% is about 80 (without Tyr). The polarity of the protein with 41 mol-% agrees with the polarity of soluble globular proteins investigated by other authors. Acid hydrolysis without preceeding performic acid oxidation gives a sum of amino acid residues of only 35--45 weight-%, the glycoprotein nature of the inhibitor could be shown by staining the SDS-gels with Schiff's reagents and by carbohydrate determination with anthrone reagent.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-5318
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
393-403
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
[Purification and characterization of the respiratory inhibitor RF from rabbit reticulocytes].
pubmed:publicationType
Journal Article, English Abstract