By Paul Berg (auth.), S. Mongkolsuk, P. S. Lovett, J. E. Trempy (eds.)
ISBN-10: 030644352X
ISBN-13: 9780306443527
ISBN-10: 0585323860
ISBN-13: 9780585323862
Eukaryotic Biotechnology: amendment particular Chromosomal Loci in Mammalian Cells via Recombination (P. Berg). transportable parts within the Human Genome (M.F. Singer). Agricultural Biotechnology: Coat Protein Mediated safeguard and the opportunity of its program in Agriculture (R.N. Beachy). constitution of Peroxidase Isozyme Gene in Brassica and their Expression (A. Shinmyo et al.). Environmental Biotechnology: Environmental keep watch over of Microbial Gene Expression and Evolution (A.M. Chakrabarty). Bacterial Heavy steel detoxing and Resistance platforms (S. Silver). Microbial Biotechnology: Induction of Cat mRNA Translation via Chloramphenicol (P.S. Lovett et al.). functions of a Multicopy Phenotype method (J.E. Trempy). New Technology: research of Epitopes within the Cholera relations of Enterotoxins (M. Kazemi, R.A. Finkelstein). 18 extra articles. Index.
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1988. Nuclear factor NF-KB can interact functionally with its cognate binding site to provide lymphoid-specific promoter function. EMBOJ. 7:31093113. 30. , and J. Piatigorsky. 1988. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Ann. Rev, Biochem. 57:479-504. 32 31. , T. Nakamura, H. Westphal, and P. Russell. 1990. Synthesis of a-crystallin by a cell line derived from thie lens of a transgenic animal. Curr. Eye Res. 9:31 -37. 32. , J. Kanellopoulos, M.
Fung. N. 303-309 9. , and Schekman, R. (1987) J. Biol. Cfiem. 282:4387-4394 10. , and Schekman, R. (1984) Mol Cell. Biol. 4:2347-2355 26 ROLE OF THE aA-CRYBP1 SITE IN LENS-SPECIFIC EXPRESSION OF THE aA-CRYSTALLIN GENE Christina M. Sax*, John F. KlemenU, Joram Platlgorsky Laboratory of Molecular and Developmental Biology, National Eye Institute National Institutes of Health, Bethesda, MD 20892 INTRODUCTION A heterogeneous group of crystallins comprise 80-90% of the soluble protein of the ocular lens and are responsible for lens transparency (see 30 for review).
The M,of glucanase protein without modification in E. co//{7) is approximately 57000 {Lane 2). The observed higher molecular mass of yeast enzyme was likely due to the glycosylation since incubation of this yeast enzyme with endo H resulted in reduction of molecular weight of the protein (data not shown). There are seven potential Nlinked glycosylation sites (7). It is unclear how many sites, and which sites are glycosylated in this protein. The yeast enzyme was found to be less active than the bacterial one.
Biotechnology and Environmental Science: Molecular Approaches by Paul Berg (auth.), S. Mongkolsuk, P. S. Lovett, J. E. Trempy (eds.)
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