Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-5-28
pubmed:abstractText
We have obtained two semisynthetic covalent hybrids (Wieczorek, M. & Laskowski, M., Jr., (1983) Biochemistry 22, 2630-2636) of turkey ovomucoid third domain by coupling the natural 19-56 peptide fragment with crude, synthetic peptides 1-18 and 6-18, respectively. We have reformed all of the disulfide bridges and then we have enzymatically synthesized the 18-19 peptide bond. The enzyme-inhibitor association constants for interaction with five different serine proteinases were the same for the semisynthetic proteins 1-56 and 6-56 and for natural proteins 1-56 and 4-56. Further, the semisynthetic 1-56 and natural 1-56 proteins were indistinguishable in analytical ion exchange and reverse-phase chromatography. This work shows that 1) making the covalent hybrids from synthetic and natural material is a facile and efficient method for preparing variants for highly quantitative sequence to reactivity studies, 2) the first five NH2-terminal residues of avian ovomucoid third domains have no effect on inhibitory activity, and 3) it is sufficient and convenient to prepare 6-56 proteins rather than 1-56 for inhibitory activity studies.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
499-504
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Covalent hybrids of ovomucoid third domains made from one synthetic and one natural peptide chain.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.