High level expression of bioactive recombinant human growth hormone in the milk of a cloned transgenic cow.

Transgenic farm animals have been proposed as an alternative to current bioreactors for large scale production of biopharmaceuticals. However, the efficiency of both methods in the production of the same protein has not yet been established. Here we report the production of recombinant human growth hormone (hGH) in the milk of a cloned transgenic cow at levels of up to 5 g l(-1).

Specific binding sites for the activator protein, ALCR, in the alcA promoter of the ethanol regulon of Aspergillus nidulans.

ALCR is the specific activator of the Aspergillus nidulans ethanol-utilization pathway, mediating the induction of its own transcription and that of the structural genes alcA and aldA, encoding respectively, alcohol dehydrogenase I and aldehyde dehydrogenase. ALCR is a DNA binding protein in which 6 cysteines are coordinated in a zinc binuclear cluster. This domain was fused to glutathione-S-transferase (GST) and isolated as a GST-ALCR(7-58*) fusion protein from Escherichia coli.

The cDNA sequence and expression of an ubiquitin-tail gene fusion in Neurospora crassa.

The genome of Neurospora crassa contains at least one natural fusion gene encoding a single ubiquitin (UBI) unit with a 78-amino acid C-terminal extension. The predominantly basic tail sequence corresponds to a highly conserved ribosomal protein identified in other organisms. The 0.

Genes responsive to the alteration of polyamine biosynthesis in neurospora crassa.

Wild-type Neurospora crassa grown in minimal medium was exposed to -difluormethyl ornithine (DFMO), a specific inhibitor of ornithine-decarboxylase (ODC-ase) activity. Protein-synthesis rates impaired by DFMO were restored by the addition of spermidine. The pattern on SDS-acrylamide gels displayed three newly synthesized polypeptides, p27, p31 and p99 after DFMO action in the absence of exogenous polyamine.

Stability of Escherichia coli strains harboring recombinant plasmids for L-threonine production.

Escherichia coli recombinant strains bearing the thr operon have been previously selected for threonine production and phenotypically classified according to antibiotic resistance properties (Nudel et al. 1987). Further analysis of those strains permitted the isolation and restriction mapping of two different plasmids of 13 kb and 18.