Search PubMed⌕ Search

Biomedical subjects

C Chiang

Publications and source records attributed to C Chiang.

60 records · Page 4Linked to original sources

Participation of H-2 regions in heart-transplant rejection.

Hearts of newborn mice were cut into small pieces, the fragments transplanted under the ear skin of adult recipients, and the graft survival followed visually (pulsating fragments were considered viable). Donor-recipient combinations were chosen from H-2 congenic (recombinant and mutant) strains in such a way as to provide differences in the entire H-2 complex or in only a small portion of it. The data obtained indicate that a difference between the donor and the recipient in either K, D, or I regions suffices for the rejection of the heart fragments. The rejection is often accompanied by the production of antibodies against classical H-2 antigens (in the case of K- or D-region disparities) or Ia antigens (in the case of I region disparities). In some instances, the antibodies persist in the recipient for more than 50 days. We conclude from these experiments that the same loci that cause acute skin graft rejection (H-2K, H-2D, and H-2I) are responsible for heart graft rejection. Furthermore, we also conclude that serologically Ia-negative tissues may carry Ia antigens in sufficient quantities to stimulate the production of Ia antibodies.

Animals↗

Purification and properties of penicillin amidase from Bacillus megaterium.

A penicillin amidase, obtained from the exogenous medium of a Bacillus megaterium culture, was purified approximately 96-fold by means of two cycles of adsorption on, and elution from, Celite, followed by a further fractionation on carboxymethylcellulose. On the basis of sedimentation centrifugation analysis, the final preparation was deemed to be homogeneous with an apparent molecular weight of approximately 120,000. The enzyme is specific for benzylpenicillin and has a pH optimum between 8 and 9. Complete hydrolysis of benzylpenicillin was obtained at low substrate concentrations. At higher substrate concentrations, the hydrolysis of benzylpenicillin was incomplete, apparently due to enzyme inhibition by phenylacetic acid and 6-aminopenicillanic acid, which were formed during the hydrolysis. Under the assay conditions, phenylacetic acid was a competitive inhibitor of penicillin amidase with an inhibitor constant (K(i)) of 0.45 m, whereas 6-aminopenicillanic acid was noncompetitive in nature with a K(i) of 2.6 x 10(-2)m. The Michaelis constant of this enzyme was found to be 4.5 x 10(-3)m when benzylpenicillin was used as substrate.

Aminohydrolases↗