| pubmed-article:8526506 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C0007961 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C1546426 | lld:lifeskim |
| pubmed-article:8526506 | lifeskim:mentions | umls-concept:C1548280 | lld:lifeskim |
| pubmed-article:8526506 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:8526506 | pubmed:dateCreated | 1996-1-25 | lld:pubmed |
| pubmed-article:8526506 | pubmed:abstractText | Three series of oligopeptides were synthesized to investigate the proposal that a major factor in determining the differences in specificity of the lactococcal cell surface-associated proteinases against caseins is the interactions between charged amino acids in the substrate and in the enzyme. The sequences of the oligopeptides were based on two regions of kappa-casein (residues 98 to 111 and 153 to 169) which show markedly different susceptibilities to PI- and PIII-type lactococcal proteinases. In each series, one oligopeptide had an identical sequence to that of the kappa-casein region, while in the others, one or more charged residues were substituted by an amino acid of opposite charge, i.e., His<-->Glu. Generally, substitution of His by Glu in the oligopeptides corresponding to residues 98 to 111 of kappa-casein resulted in reduced cleavage of susceptible bonds by the PI-type proteinase and increased cleavage of susceptible bonds by the PIII-type proteinase. In the case of the oligopeptide corresponding to residues 153 to 169 of kappa-casein, one major cleavage site was evident, and the bond was hydrolyzed by both types of proteinase (even though this sequence in kappa-casein itself is extremely resistant to the PI-type enzyme). Substitution of Glu by His in this oligopeptide, even in the P7 position, resulted in increased cleavage of the bond by the PI-type proteinase and reduced cleavage by the PIII-type proteinase. C-terminal truncation of this oligopeptide resulted in a 100-fold decrease in the rate of hydrolysis of the susceptible bond and a change in the pattern of cleavage.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8526506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8526506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8526506 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8526506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8526506 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8526506 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:8526506 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:8526506 | pubmed:author | pubmed-author:PritchardG... | lld:pubmed |
| pubmed-article:8526506 | pubmed:author | pubmed-author:ReidJ RJR | lld:pubmed |
| pubmed-article:8526506 | pubmed:author | pubmed-author:MooreC HCH | lld:pubmed |
| pubmed-article:8526506 | pubmed:author | pubmed-author:HardingD RDR | lld:pubmed |
| pubmed-article:8526506 | pubmed:author | pubmed-author:CoolbearTT | lld:pubmed |
| pubmed-article:8526506 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8526506 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:8526506 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8526506 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8526506 | pubmed:pagination | 3934-9 | lld:pubmed |
| pubmed-article:8526506 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:meshHeading | pubmed-meshheading:8526506-... | lld:pubmed |
| pubmed-article:8526506 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8526506 | pubmed:articleTitle | Involvement of enzyme-substrate charge interactions in the caseinolytic specificity of lactococcal cell envelope-associated proteinases. | lld:pubmed |
| pubmed-article:8526506 | pubmed:affiliation | New Zealand Dairy Research Institute, Palmerston North, New Zealand. | lld:pubmed |
| pubmed-article:8526506 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8526506 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8526506 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
