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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1994-4-12
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pubmed:abstractText |
The metabolism of the endogenous brain peptides Tyr-MIF-1 (Tyr-Pro-Leu-Gly-NH2) and MIF-1 (Pro-Leu-Gly-NH2) was determined by HPLC after incubation of the tritiated peptides in human and rat plasma. Degradation of Tyr-MIF-1 was rapid in the plasma from both species, in contrast to the slightly delayed degradation of MIF-1 in rat plasma and the extremely prolonged persistence of MIF-1 in human plasma. In rat plasma, more than half of the intact Tyr-MIF-1 and MIF-1 was degraded within 5 min, in contrast to the 5 days required for 50% degradation of MIF-1 in human plasma at 37 degrees. To slow the rapid rate of metabolism, studies were then performed at 0 degree. Incubation of Tyr-MIF-1 in human plasma at 0 degree for 2 hr resulted in HPLC identification of more Tyr-Pro than Tyr at all times. At 0 degree in rat plasma, however, more Tyr than Tyr-Pro was formed after the first 5 min of incubation of the Tyr-MIF-1 that was labeled on the Tyr. This raised the possibility that the tetrapeptide Tyr-MIF-1 might be serving as a precursor of the tripeptide MIF-1. Incubation of Tyr-MIF-1 tritiated at the Pro under the same conditions with and without Tyr-MIF-1 tritiated at the Tyr showed that Tyr-Pro, not MIF-1, was the predominant degradation product of Tyr-MIF-1. In addition to the metabolism of Tyr-MIF-1 being slower at lower temperatures, it was also slowed by some enzyme inhibitors. After 10 min of incubation at 37 degrees, EDTA appeared to be more effective than bestatin, p-chloromercuribenzoic acid (PCMB), pepstatin, or aprotinin, but after 30 min, bestatin was more effective. Intravenous injection of the tritiated peptides into rats showed short half-time disappearances; again, MIF-1 persisted in blood longer than Tyr-MIF-1. Thus, the results show the rapid metabolism of Tyr-MIF-1 in human and rat plasma, the slightly slower metabolism of MIF-1 in rat plasma, the predominant formation of Tyr-Pro rather than MIF-1 from Tyr-MIF-1, and the markedly delayed metabolism of MIF-1 in human plasma.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-2952
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
699-709
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7907473-Amino Acid Sequence,
pubmed-meshheading:7907473-Animals,
pubmed-meshheading:7907473-Enzyme Inhibitors,
pubmed-meshheading:7907473-Humans,
pubmed-meshheading:7907473-MSH Release-Inhibiting Hormone,
pubmed-meshheading:7907473-Male,
pubmed-meshheading:7907473-Molecular Sequence Data,
pubmed-meshheading:7907473-Rats,
pubmed-meshheading:7907473-Temperature,
pubmed-meshheading:7907473-Time Factors,
pubmed-meshheading:7907473-Tritium
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pubmed:year |
1994
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pubmed:articleTitle |
Differential metabolism of Tyr-MIF-1 and MIF-1 in rat and human plasma.
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pubmed:affiliation |
VA Medical Center, New Orleans, LA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.
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