| pubmed-article:9652393 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C0023047 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C0019051 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C1706124 | lld:lifeskim |
| pubmed-article:9652393 | lifeskim:mentions | umls-concept:C1004460 | lld:lifeskim |
| pubmed-article:9652393 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9652393 | pubmed:dateCreated | 1998-7-28 | lld:pubmed |
| pubmed-article:9652393 | pubmed:abstractText | Previously, we purified and characterized a pro-phenol-oxidase (pro-PO) of 79 kDa from coleopteran insect, Holotrichia diomphalia larvae [Kwon et al. (1997) Mol. Cells 7, 90-97]. Here, we describe the identification of two pro-PO-activating factors (PPAF), named PPAF-I and PPAF-II, directly involved in the activation of the isolated pro-PO. When pro-PO was incubated with either PPAF-I or PPAF-II, no phenol oxidase activity was observed. However, incubation of pro-PO with both PPAF-I and PPAF-II specifically exhibited phenol oxidase activity. The purified PPAF-I with a molecular mass of 33 kDa on SDS/PAGE had characteristics of a serine protease. It exhibited amidase activity against fluorogenic peptide substrates, tert-butoxycarbonyl-phenylalanyl-seryl-arginyl-4-methylcoumaryl-7-amide being the best among the substrates examined. The activity was completely inhibited by 0.02 mM p-nitrophenyl-p'-guanidinobenzoate HCl and diisopropylflurophosphate. The NH2-terminal sequence of PPAF-I had significant sequence similarity to those of serine proteases. On the other hand, the purified PPAF-II had a molecular mass of 40 kDa on SDS/PAGE and 400 kDa determined by gel filtration, indicating an oligomeric protein. The NH2-terminal sequence of PPAF-II showed no similarity to known proteins. PPAF-II exhibited no amidase activity against the fluorogenic substrates. Reconstitution experiments and immunoblotting analysis using affinity-purified antibody against pro-PO demonstrated that PPAF-I first cleaves the intact pro-PO to an intermediate of 76 kDa with no phenol oxidase activity, and then, PPAF-I converts the intermediate to the active phenol oxidase of 60 kDa in the presence of PPAF-II. These results indicate that the activation of pro-PO system in hemolymph of H. diomphalia larvae is accomplished by at least two activating factors, a serine protease and a protein cofactor. | lld:pubmed |
| pubmed-article:9652393 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9652393 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9652393 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9652393 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9652393 | pubmed:month | May | lld:pubmed |
| pubmed-article:9652393 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:IwanagaSS | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:LeeS YSY | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:MANNM VMV | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:LeeB LBL | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:HyunJ HJH | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:ChoiJ SJS | lld:pubmed |
| pubmed-article:9652393 | pubmed:author | pubmed-author:KawabataS ISI | lld:pubmed |
| pubmed-article:9652393 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9652393 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:9652393 | pubmed:volume | 254 | lld:pubmed |
| pubmed-article:9652393 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9652393 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9652393 | pubmed:pagination | 50-7 | lld:pubmed |
| pubmed-article:9652393 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:9652393 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9652393 | pubmed:articleTitle | In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae. | lld:pubmed |
| pubmed-article:9652393 | pubmed:affiliation | College of Pharmacy, Pusan National University, Kumjeong Ku, Korea. | lld:pubmed |
| pubmed-article:9652393 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9652393 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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