Protein L is a cell-surface protein from Peptostreptococcus which inte
racts with immunoglobulin kappa light chains. A gene from Peptostrepto
coccus strain 3316 coding for protein L and fragments thereof were exp
ressed in Escherichia coli. The peptides were examined for binding to
immunoglobulin and serum albumin. The four C units were shown to be re
sponsible for binding to immunoglobulin and the four D units for bindi
ng to albumin. This protein L molecule therefore binds to albumin at a
site separate from that involved in binding to immunoglobulin. The al
bumin-binding units have high amino acid sequence identity with the al
bumin-binding units of streptococcal cell-surface proteins. The gene c
ontains three sites available for Internal initiation of translation r
esulting in three active proteins. The protein L molecule presented in
this report was compared with a previously reported protein from Pept
ostreptococcus strain 312. The two proteins differ in several respects
, including size and the number and types of repeat units.