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PubMed1964

THE EVOLUTION OF THE IMMUNE RESPONSE. 3. IMMUNOLOGIC RESPONSES IN THE LAMPREY.

1. Studies of the immune response have been carried out in more than 1700 lampreys representing three stages in the life cycle of these animals. 2. Lampreys used in this study were unable to clear certain soluble protein antigens and bacteriophage and were unable to make antibodies to these antigens. Hemocyanin was cleared from the circulation. 3. The immune responses demonstrated in lampreys include the production of specific antibody to killed Brucella cells, the rejection of skin homografts, and the development of a delayed allergic response to old tuberculin. 4. A responsive proliferation of lymphoid cells occurred in the protovertebral arch following antigen-adjuvant stimulation. 5. Electrophoretic and immunoelectrophoretic analysis of lamprey serum revealed gamma globulin. Ultracentrifugal analysis of serum revealed proteins with sedimentation coefficients of 17S, 8S, 7S, and 3S. 6. The antibodies thus far observed in the lamprey are of relatively high molecular weight and destroyed by 2-mercaptoethanol. 7. In the lamprey it would appear that there is reflected the coordinate evolution of a primitive thymus, primitive spleen containing lymphoid foci, a family of lymphocytes in the peripheral blood and capacity for gamma globulin synthesis and expression of adaptive immunity.

Animals↗

PubMed1965

THE INHERITANCE OF THE PROTEIN AND NUCLEIC ACID CHARACTERISTICS OF T2 AND T6 BACTERIOPHAGE.

A study of the immunological properties of phage strains derived from T2 x T6 crosses revealed that the majority of the progeny differ serologically from the parental viruses. Some hybrids were found to contain head membranes having the serological specificity of both T2 and T6 phages, while others contained tail sheaths of the former and the tail fibers of the latter. Since the immunological properties of all hybrids were heritable, it has been concluded that the serological specificity of the head proteins of T2 and T6 is controlled by at least two genetic determinants, and that the specificities of the fiber and sheath proteins may be governed by single genes. Furthermore it was found that nucleic acids of hybrids had similar proportions of unsubstituted, mono- and diglucosylated hydroxymethylcytosine nucleotides to the nucleic acid of either T2 or T6 phage. Since the parental and hybrid viruses having chemically similar nucleic acids contained in some instances serologically different proteins, it has also been concluded that the extent of glucosylation of the hydroxymethylcytosine component of viral nucleic acids and the immunological properties of viral proteins are independently heritable traits of T2 and T6 bacteriophages.

Bacteriophages↗

PubMed1965

ENHANCEMENTS OF ANTIBIOTIC ACTIVITY OF COLICINE K AND ALTERATION OF SEROLOGICAL PROPERTIES OF COLICINE K AND ENDOTOXINS.

Hemoglobin, its chains, and myoglobin enhance the antibiotic activity of colicine K. These proteins also interact with colicine K and other O antigens to alter their serological activity. The hemoglobin proteins did not alter the serological activities of three Pneumococcus polysaccharides or T4 bacteriophage DNA antigens but did alter the antigenic activity of fetuin. Interaction of hemoglobin and colicine K resulted in a retardation of colicine K antibiotic moiety as measured by gel filtration but did not affect the gel filtration properties of the lipopolysaccharide moiety.

Anti-Bacterial Agents↗

PubMed1964

THE EFFECT OF PROTEOLYTIC ENZYMES ON E. COLI PHAGES AND ON NATIVE PROTEINS.

Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T(2) phage is slowly inactivated by high concentrations of (alpha-, beta-, gamma-, or Delta-chymotrypsin, but not by trypsin or ficin. P(1) phage is slowly inactivated by alpha-, beta-, or gamma-chymotrypsin, or ficin, more rapidly by Delta-chymotrypsin, and much more rapidly by trypsin. Crystalline egg albumin, crystalline serum albumin, E. coli nucleoprotein, and yeast nucleoprotein are hydrolyzed slowly by alpha-chymotrypsin. Yeast nucleoprotein, like P(1) phage, is hydrolyzed more rapidly by Delta-chymotrypsin than by alpha-chymotrypsin, but not by trypsin or ficin. Neither phages nor native proteins were attacked by papain, carboxypeptidase, deoxyribonuclease, or ribonuclease.

Bacteriophages↗

PubMed1962