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Physikalisch‐chemische, chemische und immunologische Eigenschaften der FDP‐Aldolase aus Drosophila melanogaster . 16. Mitteilung über Aldolasen [1]
Author(s) -
BrennerHolzach O.,
Leuthardt F.
Publication year - 1969
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19690520513
Subject(s) - aldolase a , chemistry , glycine , histidine , microbiology and biotechnology , biochemistry , stereochemistry , amino acid , enzyme , biology
The properties of pure aldolase from pupae of Drosophila melanogaster have been studied: The molecular weight is about 159000 ( s 20, w 0= 7.81 S, D 20, w 0= 4.55 · 10 −7 ). From the frictional ratio f / f 0 = 1.236 the axial ratio for an oblong non hydrated ellipsoid of rotation can be calculated as b / a = 4.74. The molecular activity is 2700 for FDP and approximately 200 for F‐1‐P. Amino acid analysis shows significant differences between Drosophila aldolase and rabbit muscle and liver aldolases, especially in the contents of histidine, glycine, alanine and cysteine. Hybridization with rabbit brain aldolase gives three new hybrids. Anti‐ Drosophila aldolase serum (guinea pig) does not precipitate rabbit muscle aldolase (type A) or rabbit brain aldolase (type C) in the O UCHTERLONY test.