The epsilon-(gamma-glutamyl)lysine moiety in crosslinked casein is an available source of lysine for rats.

To determine bioavailability, expressed as the protein efficiency ratio (PER) and biological value (BV) in rats, of the epsilon-(gamma-glutamyl)lysine [epsilon-(gamma-Glu)Lys] moiety in crosslinked proteins, we prepared heavily crosslinked [21.5 /micromol epsilon-(gamma-Glu)Lys/g casein] and intermediately crosslinked [13.6 micromol epsilon-(gamma-Glu)Lys/g casein] casein, using microbial transglutaminase. In Experiment 1, rats were assigned to one of four diets (heavily or intermediately crosslinked caseins, intact casein or non-protein diet) for 4 wk to evaluate the bioavailability of the epsilon-(gamma-Glu)Lys moiety in crosslinked casein as the sole source of dietary protein. Rats that were fed intact casein and the two crosslinked caseins had similar growth rates, PER, and BV, indicating that crosslinked caseins supported the growth of rats similarly to the intact casein. In Experiment 2, heavily crosslinked casein was added to wheat gluten-based diets in concentrations of 20 and 40 g/kg diet to evaluate the bioavailability of lysine in the epsilon-(gamma-Glu)Lys moiety of the casein as a lysine supplement for lysine-poor gluten. One of six diets (heavily crosslinked or intact casein diets in the two concentrations, gluten diet, or non-protein diet) was fed to rats for 4 wk. No significant differences in food intake, body weight gain, PER or BV were observed among rats fed the intact or crosslinked casein diets at either 2 or 4 g/100 g casein. These results suggest that the epsilon-(gamma-Glu)Lys moiety in crosslinked caseins are absorbed and therefore supplement the gluten. HPLC analysis of urine and feces of rats fed the crosslinked caseins actually confirmed that approximately 99% of the epsilon-(gamma-Glu)Lys moiety was absorbed in the body.

Cell-adhesive immunoglobulin M in human plasma.

Human plasma contains a cell-adhesive protein that has a structure related to immunoglobulins. This protein was purified by affinity chromatography on an elastin-Sepharose column and by Mono Q anion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing and reducing conditions revealed that this protein is a kind of immunoglobulin M (IgM). Antibodies against the mu chain and against the Fc region of IgM inhibited the adhesion of cells to this protein. Addition of the peptide GRGDS into media inhibited the adhesion, too. These results suggest that this protein is a special subset of IgM having a cell-binding sequence in the Fc region. We propose the name "cell-adhesive immunoglobulin M (CA-IgM)" for this protein. CA-IgM binds to alpha-elastin and laminin suggesting that it may play a role in the interaction between cells and the extracellular matrix.