S. Yamamato et al., OCCURRENCE AND ANTIGENIC HETEROGENEITY OF L-2,4-DIAMINOBUTYRATE DECARBOXYLASE IN ACINETOBACTER SPECIES, Biological & pharmaceutical bulletin, 18(3), 1995, pp. 454-456
We have previously reported that a novel enzyme, L-2,4-diaminobutyrate
decarboxylase (DABA DC), which is responsible for the formation of 1,
3-diaminopropane, occurs in two Acinetobacter species. The present stu
dy extends this observation to additional Acinetobacter species and st
rains (6 reference strains and 30 clinical isolates). Furthermore, the
DABA DC protein was detected in every strain by Western blot analysis
with the antiserum against the enzyme purified from A. baumannii ATCC
19606. However, only the DABA DCs in the A. calcoaceticus and Acineto
bacter genospecies 3 in addition to A. baumannii strains strongly cros
s-reacted with the antiserum, suggesting antigenic heterogeneity among
the DABA DC proteins in Acinetobacter species. Therefore, immunologic
al testing of the DABA DC protein may provide an additional method for
differentiating and identifying Acinetobacter strains.