| pubmed-article:8600179 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C1415800 | lld:lifeskim |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C0302891 | lld:lifeskim |
| pubmed-article:8600179 | lifeskim:mentions | umls-concept:C0442040 | lld:lifeskim |
| pubmed-article:8600179 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8600179 | pubmed:dateCreated | 1996-4-26 | lld:pubmed |
| pubmed-article:8600179 | pubmed:abstractText | Histatin 1 is a histidine-rich phosphoprotein present in human parotid saliva that possesses candidacidal activity and functions in mineralization by adsorbing to hydroxyapatite. The objective of the present study was to develop a system for recombinant production of histatin 1 and to examine the role of phosphorylation in the functional activities of this molecule. Native histatin 1 (containing a phosphoserine at residue 2) was purified from parotid saliva, whereas a bacterial expression system was used to produce a recombinant form of histatin 1 (re-Hst1) that lacked phosphorylated serine. Histatin 1 cDNA was inserted into the vector pGEX-3X, which expresses foreign genes as soluble fusion proteins attached to the carboxyl-terminus of glutathione S-transferase (GST). The GST/re-Hst1 fusion protein was isolated from cell lysates by affinity chromatography on glutathione (GSH)-Sepharose and digested with cyanogen bromide to separate re-Hst1 from the GST fusion partner. The digest was subjected to reversed-phase high-performance liquid chromatography on a C18 column, and re-Hst1 was eluted as a well-defined peak. The yield of re-Hst1 was 4 mg/L of bacterial culture. Amino-terminal sequencing and amino acid analysis confirmed the final product as re-Hst1. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed that native histatin 1 and re-Hst1 had the same apparent molecular weights, while cationic PAGE showed that re-Hst1 was more basic. Phosphate analysis indicated 1 mol phosphate/mol of native histatin 1, while re-Hst1 lacked any detectable phosphate. Re-Hst1 demonstrated candidacidal activity comparable to that of native histatin 1, but displayed substantially lower binding to hydroxyapatite. These results show that phosphorylation of histatin 1 at residue 2 contributes significantly to its ability to bind to hydroxyapatite. | lld:pubmed |
| pubmed-article:8600179 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8600179 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8600179 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8600179 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8600179 | pubmed:citationSubset | D | lld:pubmed |
| pubmed-article:8600179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8600179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8600179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8600179 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8600179 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8600179 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8600179 | pubmed:issn | 0022-0345 | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:TroxlerR FRF | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:OppenheimF... | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:DriscollJJ | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:GAYJ LJL | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:ZuoYY | lld:pubmed |
| pubmed-article:8600179 | pubmed:author | pubmed-author:ChoiJ RJR | lld:pubmed |
| pubmed-article:8600179 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8600179 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:8600179 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8600179 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8600179 | pubmed:pagination | 1837-44 | lld:pubmed |
| pubmed-article:8600179 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8600179 | pubmed:meshHeading | pubmed-meshheading:8600179-... | lld:pubmed |
| pubmed-article:8600179 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8600179 | pubmed:articleTitle | Functional comparison of native and recombinant human salivary histatin 1. | lld:pubmed |
| pubmed-article:8600179 | pubmed:affiliation | Department of Periodontology and Oral Biology, School of Graduate Dentistry, Boston University Medical Center, MA 02118, USA. | lld:pubmed |
| pubmed-article:8600179 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8600179 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8600179 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:3346 | entrezgene:pubmed | pubmed-article:8600179 | lld:entrezgene |
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