Abstract:
Histone Hlt has been purified from rat testes and
antibodies were elicited in rabbits. Immunoblotting
studies with anti-histone Hlt-IgG have shown that it
reacted specifically with histone Hlt but not with other
histone H1 subtypes, namelyH la, -b, -c, -d, -e and HlO.
The anti-histone Hlt-IgG also did not react with
chicken erythrocyte histone H5. Immunoblotting studies
have also revealed that the polyclonal anti-histone
Hlt-IgG reacted with (a) two polypeptide fragments,
NBS-N and NBS-C, derived from N-bromosuccinimide
cleavage of histoneH lt, (b)t wo polypeptide fragments,
CT-N and CT-C, derived from a-chymotrypsinc leavage
of histone Hlt, and (c) GHlt, globular domain of
histone Hlt obtained after trypsin cleavage. The indirect
immunofluorescence studies on nuclei isolated
from adult ratet stes with anti-histoneH lt-IgG showed
that the fluorescence, particularly, of the pachytene
nucleus was the brightest. On the other hand, antihistone
Hlt-IgG did not stain nuclei from either liver
or nuclei isolated fromth e testes of 10-day-old rats.