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Free and bonded homoisoleucine in sclerotia of the parasitic fungus Claviceps purpurea.

Authors :
Jegorov, A.
Šimek, P.
Heydová, A.
Cvak, L.
Minář, J.
Source :
Amino Acids; Jan1997, Vol. 12 Issue 1, p9-19, 11p
Publication Year :
1997

Abstract

Homoisoleucine, an unusual amino acid recently discovered in the structure of the ergopeptine alkaloid ergogaline, was determined in the parasitic fungus Claviceps purpurea Fr. (Tul.). growing on rye Secale cereale (L.) and in its host plant. Free homoisoleucine was detected by gas chromatography-mass spectrometry (GC-MS) in the amino acid pool of sclerotia of all fungal strains examined. Since homoisoleucine was not detected in rye, it seems that the amino acid is synthetized by the fungus. Furthermore, the ratio of leucine/homoisoleucine in the free amino acid pool of sclerotia is in good agreement with the ratio of the corresponding alkaloids α-ergokryptine/ergogaline estimated by high performance liquid chromatography (HPLC). Thus, homoisoleucine is incorporated into the ergopeptines randomly with the similar specificity as leucine. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
09394451
Volume :
12
Issue :
1
Database :
Complementary Index
Journal :
Amino Acids
Publication Type :
Academic Journal
Accession number :
49939144
Full Text :
https://doi.org/10.1007/BF01373422