| pubmed-article:8936307 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8936307 | lifeskim:mentions | umls-concept:C0029235 | lld:lifeskim |
| pubmed-article:8936307 | lifeskim:mentions | umls-concept:C0317592 | lld:lifeskim |
| pubmed-article:8936307 | lifeskim:mentions | umls-concept:C0002570 | lld:lifeskim |
| pubmed-article:8936307 | lifeskim:mentions | umls-concept:C0036782 | lld:lifeskim |
| pubmed-article:8936307 | lifeskim:mentions | umls-concept:C1547276 | lld:lifeskim |
| pubmed-article:8936307 | pubmed:dateCreated | 1996-12-31 | lld:pubmed |
| pubmed-article:8936307 | pubmed:abstractText | An aminopeptidase with a very broad substrate specificity was purified to homogeneity from Lactobacillus helveticus SBT 2171 by FPLC. The enzyme was purified 144-fold from a cell-free extract with a yield of 16%. The purified enzyme appeared as a single band on an SDS-PAGE gel. It had a molecular mass of 95 kDa and an isoelectric point of 4.9. The enzyme hydrolysed a large range of naphthylamide- and nitroanilide-substituted amino acids, as well as several di-, tri- and oligopeptides. It also exhibited significant proline-iminopeptidase-like activity, since it hydrolysed several proline-containing peptides. Prolyl-p-nitroanilide was hydrolysed with a low affinity (Michaelis-Menten constant 0.6 mM) and a Vmax of 2.5 mumol min-1 (mg protein)-1 while lysyl-p-nitroanilide was hydrolysed with a high affinity [Km 0.003 mM; Vmax 37.5 mumol min-1 (mg protein)-1]. The aminopeptidase activity, which was optimal between pH 6.0 and 8.0 and at 50 degrees C, was very stable at 30 degrees C for more than 7 d. The activity lost by treatment with the thiol-blocking reagents could be restored with beta-mercaptoethanol, while Co2+ and Mn2+ restored the activity of the EDTA-treated enzyme. Immunological experiments with antibodies raised against the aminopeptidases from Lactococcus lactis and Lb. helveticus clearly showed that both aminopeptidases are at least immunologically different from each other. | lld:pubmed |
| pubmed-article:8936307 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8936307 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8936307 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8936307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8936307 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8936307 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8936307 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8936307 | pubmed:issn | 1350-0872 | lld:pubmed |
| pubmed-article:8936307 | pubmed:author | pubmed-author:SasakiMM | lld:pubmed |
| pubmed-article:8936307 | pubmed:author | pubmed-author:TanP SPS | lld:pubmed |
| pubmed-article:8936307 | pubmed:author | pubmed-author:BosmanB WBW | lld:pubmed |
| pubmed-article:8936307 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8936307 | pubmed:volume | 142 ( Pt 4) | lld:pubmed |
| pubmed-article:8936307 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8936307 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8936307 | pubmed:pagination | 799-808 | lld:pubmed |
| pubmed-article:8936307 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:meshHeading | pubmed-meshheading:8936307-... | lld:pubmed |
| pubmed-article:8936307 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8936307 | pubmed:articleTitle | A new, broad-substrate-specificity aminopeptidase from the dairy organism Lactobacillus helveticus SBT 2171. | lld:pubmed |
| pubmed-article:8936307 | pubmed:affiliation | Snow Brand European Research Laboratories, Groningen, Netherlands. | lld:pubmed |
| pubmed-article:8936307 | pubmed:publicationType | Journal Article | lld:pubmed |
