The human growth hormone (hGH) and human prolactin (hPRL) were iodinated with 125I using the lactoperoxidase method and purified by gel filtration on a Sephadex G-100 column and by ion exchange chromatography on a diethyl-aminoethyl (DEAE) cellulose column. Aliquots of the peak fraction on the Sephadex G-100 column and each fraction on the DEAE cellulose column were tested by radioimmunoassay (...

Cystine reduction in Streptococcus agalactiae, resulting in sulfhydryl formation, may account for antagonism of the antibacterial effect of lactoperoxidase-thiocyanate-hydrogen peroxide when cystine is present in excess of the amount needed for maximum growth. Accumulation of cystine by S. agalactiae and its reduction to form sulfhydryl compounds were demonstrated. The reduction of cystine appe...

Ribosomal proteins L7 and L12 are involved in the initiation, elongation and termination of polypeptide synthesis [l-6]. These acidic proteins do not function independently, but act in concert with the ribosome to perform the above steps. These observations suggest that L7 and L12 are necessary to maintain the conformational integrity of the ribosome, and that loss of ribosomal activity followi...

Human milk was subjected to heat treatments of graded severity and examined for its content of immunoglobulins, lactoferrin, lysozyme, vitamin B12-and folate-binder proteins, and lactoperoxidase. Holder pasteurization (62.5degrees C 30 minutes) reduced the IgA titer by 20%, and destroyed the small content of IgM and most of the lactoferrin. Lysozyme was stable to this treatment, but with an inc...

The in vivo evidence of the antimicrobial and antiviral activity of bovine milk and colostrum derived components are reviewed with special emphasis on lactoferrin and lactoperoxidase. Their mode of action and the rationale for their application in efficacy trials with rodents, farm animals, fish and humans, to give protection against infectious agents, are described. A distinction is made betwe...

The haem prosthetic group of lactoperoxidase can be prepared from the enzyme in high yield by reductive cleavage with mercaptoethanol in 8 M-urea under mild conditions. The product yields porphyrins, after removal of iron, which show visible spectroscopic properties similar to protoporphyrin but are considerably more polar. In the presence of iodoacetamide, a different product is obtained by re...