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In order to study the elastin-binding factors in blood, human plasma was applied to an alpha-elastin-Sepharose column. The column-binding fraction contained a 37-kDa protein, which was tentatively named EBP-37. Partial amino acid sequences of EBP-37 were determined. It had collagenous and non-collagenous domains. Homology searches of the sequences revealed that the protein is very similar but not identical to ficolins, transforming growth factor-beta 1 (TGF-beta 1)-binding proteins from porcine uterus membranes. Direct interaction of EBP-37 with elastin was confirmed by demonstrating the binding of the isolated EBP-37 to alpha-elastin on a nitrocellulose membrane using the EBP-37-specific antiserum. The existence of oligomers and multimers crosslinked by disulfide bonds was demonstrated by immunoblot analysis. Possible functions of EBP-37 are discussed.

A novel elastin-binding protein, EBP-37, was recently identified and purified from human plasma. Its partial amino acid sequences showed significant homology to porcine ficolins, which were originally purified from porcine uterus membranes as multimeric proteins with fibrinogen- and collagen-like domains. Here we report the presence of ficolins in an elastin-binding fraction of porcine plasma and the direct binding of recombinant porcine ficolin-alpha to elastin. In addition, a cDNA encoding a human counterpart of porcine ficolins that is composed of 319 amino acids and is different from EBP-37 was cloned and named human ficolin-1. Northern blotting of various human tissues revealed that human ficolin-1 mRNA is highly expressed in peripheral blood leukocytes. These data suggested that there are at least two kinds of ficolin-related proteins in both pig and human, and they may function as plasma proteins with elastin-binding activities.

Free D-amino acids were determined on the 60 fermented fish sauces collected from Southeast and East Asia. Of major D-amino acids, D-alanine, D-aspartate, and D-glutamate, D-alanine was the most abundant and found in almost all fish sauces. Fish sauces from Myanmer contained significantly higher amounts of these D-amino acids than those from six other countries. In fish sauces differing in the fer mentation periods, D-alanine and D-aspartate were highest in the over-aged fish sauce fermented for 22 months.In the 20%-salted fish sauces prepared from sardine and squid, D-alanine increased only in squid preparation in small amount. In the 10%-salted preparations, the D-alanine increase was large in squid preparation along with the high and long lasted viable bacterial count. This increase was largely sup pressed in the case of sardine preparation.All of the other fermented fish products also contained D-alanine which varied largely with products and a small amount of D-aspartate. These data indicate that at least D-alanine use is possible as a molecular marker of bacterial activities in the fermented fish products of low salt concentration.