1991 Fiscal Year Final Research Report Summary
A new protamine-specific-metalloproteinase from Penicillium
| Project/Area Number |
02660075
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
応用生物化学・栄養化学
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| Research Institution | Tohoku University |
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Principal Investigator |
ICHISHIMA Eiji Tohoku Univ. Agric. Professor, 農学部, 教授 (60015063)
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| Project Period (FY) |
1990 – 1991
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| Keywords | Metalloproteinase / Neutral Proteinase / Penicillium / Protase / Specificity |
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| Research Abstract |
It was found that a metalloproteinase from Penicillium citrinum has a specificity unique from those of other metalloproteinases on nuclear basic proteins and oxidized insulin B-chain.
The enzyme was found to contain 1 gram-atom zinc per mole of enzyme with the molecular weight of 17, 000. About 95% of the amino acid sequence of the enzyme was determined. The circular dichroism(CD)of the holo- and apo-enzymes has been investigated. One gram-atom of zinc was essential component of the enzyme not only the activity but also the conformation.
The enzyme was specifically active on basic nuclear protein& such as clupeine, salmine and histone at pH 7.0. The initial site of cleavage on the oxidized insulin B-chain by the proteinase was between Tyrl6-Leul7, and additional sites, Glul3-Alal4 and Alal4-Leul5 were noted. Hydrolyses of small peptides consisting 5 - 13 amino acids such as bradykinin, dynorphin-A, alpha-neoendorphin, neurotensin, luteinizing hormone releasing hormone, alpha-melanocyt. e stimulating hormone, substance P and chicken brain pentapeptide were noted.
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