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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1984-10-19
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pubmed:abstractText |
A peroxidase with stability, chromatographic and immunoreactive properties similar to that of bovine lactoperoxidase has been partly purified from human colostrum. Hydrophobic interaction chromatography on Phenyl-Sepharose C1-4B gave a 10-fold purification with an apparent recovery of about 45%. The enzyme was quantitatively and specifically adsorbed to beads of anti-lactoperoxidase (bovine)-Protein A-Sepharose. No adsorption of the enzyme was observed on immunoadsorbent columns prepared with high-titre polyclonal antibodies raised against human myeloperoxidase and human eosinophile peroxidase.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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|
pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
174
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
300-3
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6205900-Chromatography, Affinity,
pubmed-meshheading:6205900-Colostrum,
pubmed-meshheading:6205900-Eosinophils,
pubmed-meshheading:6205900-Epitopes,
pubmed-meshheading:6205900-Humans,
pubmed-meshheading:6205900-Immunosorbent Techniques,
pubmed-meshheading:6205900-Isoenzymes,
pubmed-meshheading:6205900-Lactoperoxidase,
pubmed-meshheading:6205900-Leukocytes,
pubmed-meshheading:6205900-Peroxidase,
pubmed-meshheading:6205900-Peroxidases
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pubmed:year |
1984
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pubmed:articleTitle |
Demonstration and partial purification of lactoperoxidase from human colostrum.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|
