[Changes in serum contents of inflammatory mediators after tetramethylene-disulfo-tetramine poisoning and clinical study of a new treatment regime for the poisoning].

Objective: To study the changes in serum contents of beta-endorphin (beta-EP), endothelins (ET), nitric oxide (NO) and tumor necrosis factor (TNF) after acute tetramethylene-disulfo-tetramine (TDT) poisoning and therapeutic effect of a new treatment regime.

Methods: (1) Forty-eight patients with tetramethylene-disulfo-tetramine poisoning (experiment group) were enrolled in this study. The serum levels of beta-EP, ET, NO and TNF were measured upon hospitalization and 1, 3, 5, 7, 9, 11, 13, 15, 17 and 19 days after poisoning, respectively, and compared with those of 30 healthy individuals (control group B).

Toxicity of two type II ribosome-inactivating proteins (cinnamomin and ricin) to domestic silkworm larvae.

Cinnamomin and ricin are two type II ribosome-inactivating proteins. They exhibited a different toxicity to domestic silkworm (Bombyx mori) larvae by oral feeding bioassay. The LC50 of ricin to the silkworm larvae at third instar was much lower than that of cinnamomin.

Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonica A).

Lamjapin, a novel type Iota ribosome-inactivating protein, has been isolated from kelp (Laminaria japonica A), a marine alga. This protein has been extensively purified through multiple chromatography columns. With a molecular mass of approximately 36 kDa, lamjapin is slightly larger than the other known single-chain ribosome-inactivating proteins from the higher plants.

Purification of alpha-sarcin and an antifungal protein from mold (Aspergillus giganteus) by chitin affinity chromatography.

A simple method for preparation of alpha-sarcin and an antifungal protein (AFP) from mold (Aspergillus giganteus MDH 18894) has been developed. alpha-Sarcin and AFP were purified simultaneously by chitin affinity column chromatography and gel filtration. By this method, 4.

Studies of three genes encoding Cinnamomin (a type II RIP) isolated from the seeds of camphor tree and their expression patterns.

Cinnamomin, which has three isoforms, is a type II ribosome-inactivating protein (RIP) purified from the mature seeds of camphor tree (Cinnamomum camphora). In a previous study, an incomplete cDNA that encoded the A- and B-chain of Cinnamomin but lacked signal peptide sequence was cloned. In the present paper, its full-length cDNA was obtained by 5' rapid amplification of cDNA ends (5'RACE).

Cinnamomin, a type II ribosome-inactivating protein, is a storage protein in the seed of the camphor tree (Cinnamomum camphora).

Cinnamomin is a novel type II ribosome-inactivating protein (RIP) isolated in our laboratory from the seed of the camphor tree (Cinnamomum camphora). In this paper the physiological role it plays in the plant cell was studied. Northern and Western blotting revealed that cinnamomin was expressed specifically in cotyledons.