Abstract:
:A HU-like protein (HBl) of Bifidobacterium longum was purified and characterized. HBl is heat-stable and acid-resistant, and has a molecular weight of about 9.1 kDa as estimated by its mobility on electrophoresis. HBl is intermediate in basicity (pI 9.8) between the HU-1 and HU-2 proteins of Escherichia coli, and is dissociated from a calf thymus DNA-cellulose column at 300-400 mM NaCl. Its amino acid composition shows many similarities with that of E coli HU. The NH2-terminal amino acid sequence of HBl also shows significant similarities to the consensus sequence deduced from the sequences of eleven HU-like proteins from prokaryotic sources. Chemical crosslinking analysis indicated that the HBl protein predominantly forms a homotypic dimer.
journal_name
Biochimiejournal_title
Biochimieauthors
Goshima N,Kano Y,Imamoto Fdoi
10.1016/0300-9084(90)90074-qsubject
Has Abstractpub_date
1990-04-01 00:00:00pages
207-12issue
4eissn
0300-9084issn
1638-6183pii
0300-9084(90)90074-Qjournal_volume
72pub_type
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