The use of tissue plasminogen activator in silicone oil-filled eyes.
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Biomedical subjects
Publications and source records attributed to F Chou.
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Peptide C1 (residues 68-88) from GP and rat BP differ by a single amino acid interchange at residue 79. This residue is serine in GP C1 and threonine in rat C1. GP C1 was encephalitogenic in Le rats at doses as low as 15 ng. Rat C1 was encephalitogenic at doses of 1,500 ng or greater. LNC from rats challenged with 25 X 10(-4) micronmol of GP C1 and 250 X 10(-4) micronmol of rat C1 showed a proliferative response in vitro to both peptides, but in each instance the magnitude of the response was greater to the GP peptide. GP C1 also induced higher levels of circulating antibodies at 25 X 10(-4) micronmol, but the specificity of antibodies produced by the two peptides was the same. These results have been interpreted as indicating that the presence of serine at position 79 in GP C1 results in the stimulation of greater numbers of T cells involved in (a) the induction of EAE, (b) the in vitro proliferative response and (c) helper function in antibody production.
A series of 15 2,5-diaziridinyl-3,6-bis(alkylamino)-1,4-benzoquinone derivatives was synthesized and evaluated as central nervous system antitumor agents in the murine intracerebral L1210 and ependymoblastoma brain tumor systems. Intraperitoneal activity was evaluted in the leukemia L1210, P388, and B16 melanocarcinoma tumor models. The more hydrophilic hydroxyalkylamino compounds were the most effective in the intraperitoneal ascites systems (L1210, P388) with the dihydroxypropylamino (18) and hydroxyethylamino (17) analogues producing long-term survivors. The simple, more lipophilic mono- and dialkylamino derivatives were most effective in the intracerebral systems. Multiple long-term survivors were obtained with the methyl (13), ethyl (14), and dimethylamino (20) compounds in the ependymoblastoma brain tumor system. The parent amino analogue 12 was very active in several tumor models. The relationship between structure, activity, and water solubility are discussed.
Amino acid sequences of encephalitogenic proteins from bovine cord and rabbit brain are reported. The bovine protein contains 45 residues. The rabbit protein is identical except for two isopolar substitutions, a dipeptide and amino acid deletion. Analysis of this protein and a 140-residue myelin basic protein indicates that the smaller protein is a portion of the larger encephalitogen. The larger myelin protein contains at least two encephalitogenic sites.