Enhancement of cell growth by expression of a cloned hemoglobin

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435 41, 435 696, 435 91, 4351723, 43525233, 4353201, 435802, 435804, 435813, 435818, 536 27, 935 11, 935 34, 935 38, 935 61, 935 67, 935 73, C12P 2102, C12P 100, C12N 1531, C12N 1567

Patent

active

050494937

DESCRIPTION:

BRIEF SUMMARY
TECHNICAL FIELD

This invention relates to the production of oxygen-binding proteins, particularly hemoglobins, and to enhancement of the growth and product synthesis characteristics of aerobic organisms in environments with sufficient as well as reduced or low levels of oxygen.
This invention relates generally to the use of recombinant DNA technology to direct or otherwise control gene expression in cultured cells, and more particularly, to methods and materials useful in subjecting the transcription and translation of DNA sequences to selective regulation by external control.


BACKGROUND ART

Globins such as hemoglobin and myoglobin are heme-containing oxygen carriers. By reversibly binding to oxygen in the presence of high oxygen concentrations and releasing it in regions or at times of low concentrations, these proteins considerably enhance the oxygen uptake rate of multicellular organisms over that allowed by mere passive diffusion. In unicellular organisms it is generally believed that the oxygen uptake rate is principally limited by the rate of transfer of dissolved oxygen in the environment or growth medium to the exterior cell surface. However, closer examination of cell structure reveals several potential diffusional barriers between environmental oxygen and the cytochromes where the oxygen finally undergoes reaction. For example, in gram negative bacteria, where the cytochromes are attached to the inside of the plasma membrane, the diffusing oxygen needs to cross transport barriers such as the cell wall, the outer membrane, the periplasmic space and the inner membrane before accepting electrons from metabolic reactions. In unicellular eucaryotes, where oxidative phosphorylation takes place in the mitochondria, there are further diffusional resistances. Small neutral molecules like oxygen are assumed to passively diffuse across these barriers; however, these barriers make a non-trivial contribution to the overall resistance to mass transfer to the actual reaction site and thus could be of significance under oxygen-limited conditions.
Physiological effects on growth due to depletion in dissolved oxygen levels has been demonstrated in the case of several organisms, including Escherichia coli, Saccharomyces cerevisiae, Pseudomonas strains, and Alcaligenes eutrophus. In E. coli for example, which has a very high affinity cytochrome, changes in dissolved oxygen tension leads to differential regulation of terminal oxidases, resulting in a decrease in the number of protons expelled per NADH molecule oxidized during aerobic respiration and, consequently, a possible adverse change in the stoichiometry of ATP biosynthesis. (Kranz et al., Journal of Bacteriology 158:1191-1194, 1984; Ingraham et al., Growth of the bacterial cell, Sinauer Associates, Inc. 1983, p. 147, both specifically incorporated herein.)
In addition to the respiratory oxygen requirement of aerobic organisms, oxygen-binding proteins have other potential applications as well, including, for example, the enhancement of particular oxidative transformations such as steroid conversions, vinegar production, biological waste treatment or enzymatic degradations, and in some steps in brewing or making distilled and fermented foods and beverages.
The filamentous bacterium, Vitreoscilla, a member of the Beggiatoa family, is a strict aerobe that is found in oxygen-poor environments such as stagnant ponds and decaying vegetable matter. Growth of the bacterium under hypoxic conditions results in a several-fold induction of synthesis of a homodimeric soluble heme protein (subunit MW 15,775) (Boerman et al., Control of heme content in Vitreoscilla by oxygen, Journal of General Applied Microbiology 28:35-42, 1982) which has a remarkable spectral (Webster, et al., Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla, Journal of Biological Chemistry 249:4257-4260, 1974), structural (Wakabayashi, et al., Primary sequences of a dimeric bacterial hemoglobin from Vitreoscilla, Nature 322:481-48

REFERENCES:
patent: 4615974 (1986-10-01), Kingsman et al.
patent: 4725535 (1988-02-01), Sonenshein et al.
patent: 4766068 (1988-08-01), Oeda et al.
Ellis, J. G., et al. 1987 EMBO Journal vol. 6, pp. 11-16.
von Bodman, S. B., et al. 1986, Proc. Nat. Acad. Sci. U.S.A. vol. 83, pp. 9443-9447.
Unger, B. P. et al., 1986, J. Biol. Chem. vol. 261 pp. 1158-1163.
Zinoni, F., et al., 1986 Proc. Nat. Acad. Sci. U.S.A. vol. 83, pp. 4650-4654.
Rosenberg et al., Ann Rev. Genetics 13 319-23 (1979).
Nishi et al., Agric. Biol. Chem. 48(3), 669-75 (1984).
Wakabayashi et al., Nature vol. 322, 481-4 1986.
Stargaard et al,, EMBO Journal vol. 6 3565-3569 (1987).
de Boer et al, Proc. Natl. Acad. Sci. vol. 80 pp. 21-25 (1983).
Boerman et al, J. Gen. App. Microbiol. 28 35-43 (1982).
Sato et al, Plasmid 6, 325 (1981).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Enhancement of cell growth by expression of a cloned hemoglobin does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Enhancement of cell growth by expression of a cloned hemoglobin , we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Enhancement of cell growth by expression of a cloned hemoglobin will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1916855

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.