Linked Life Data

8954527

Source:http://linkedlifedata.com/resource/pubmed/id/8954527

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-3-24
pubmed:abstractText
Peptide mapping using proteolytic enzymes is one useful technique to characterize proteins. However, developing an optimized peptide map is empirical. Some proteins are resistant to proteolysis and it is thereby difficult to obtain a good peptide map. In many cases, the protease-to-substrate ratio is the first modifier to improve the peptide map. As a consequence of increasing the amount of protease, some complications such as nonspecific cleavage, disulfide interchange, transpeptidation, and autolysis of the protease itself may occur. Recombinant human insulin-like growth factor-I (r-HuIGF-I) has been shown to generate a transpeptidation product and a nonspecifically cleaved product under the conditions reported in the literature. We describe here the completion of a peptide map using a combination of Asp-N and Glu-C (V8 strain) endoproteinases. No apparent transpeptidation, nonspecific cleavage, and disulfide exchange was observed. In situ digest of r-HuIGF-I on the probe was also analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and proved to be a quick method to analyze the sample.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
243
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
74-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Preventing the generation of artifacts during peptide map analysis of recombinant human insulin-like growth factor-I.
pubmed:affiliation
Amgen Inc., Amgen Center, Thousand Oaks, California 91320, USA.
pubmed:publicationType
Journal Article