Processes for producing pre-prorennin, prorennin and rennin

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

4351723, 435226, 435243, 4352523, 43525233, 4352542, 43525411, 43525421, 4353201, 536 235, 935 14, 935 68, 935 69, 935 72, 935 73, C12P 2106, C12N 1500, C12N 1512

Patent

active

054967112

ABSTRACT:
Living cells containing genetic material derived from recombinant DNA material and capable of expressing rennin, pre-prorennin and prorennin. The rennin, pre-prorennin and prorennin are derived from cells which are themselves or have had parents thereof treated by recombinant DNA methods to allow production of the desired enzymatic proteins during growth in culture.

REFERENCES:
patent: 4136201 (1979-01-01), Feldman
patent: 4322499 (1982-03-01), Baxter et al.
patent: 4332892 (1982-06-01), Ptashne et al.
patent: 4338397 (1982-07-01), Gilbert et al.
patent: 4349629 (1982-09-01), Carey et al.
patent: 4370417 (1983-01-01), Hung et al.
patent: 4387162 (1983-06-01), Aigle et al.
Foltman, Methods in Engmology, vol. 19, pp. 431-436 (1970) Academic Press, N.Y.
Houghton et al, Nucl. Acids Res. 8 (May 10, 1980), 1913.
Uchiyama et al, Agric. Biol. Chem., 44(6) 1373 (Jun. 1980).
Jalmadge et al, Proc. Natl. Acad. Sci. USA; 77(7) 1980, 3988-92.
Guarente et al., Chem. Abs. 93 (1980) 65844t.
R. Higuchi et al., "A general method for cloning eukaryotic structural gene sequences", Proc. Natl. Acad. Sci. USA 73(9):3146-3150 (1976).
M. Rose et al., "Yeast genes fused to .beta.-galactosidase in Escherichia coli can be expressed normally in yeast", Proc. Natl. Acad. Sci. USA 78(4):2460-2464 (1981).
L. Guarente and M. Ptashne, "Fusion of Escherichia coli lacZ to the cytochrome c gene of Saccharomyces cervisiae", Proc. Natl. Acad. Sci. USA 78(4):2199-2203 (1981).
R. W. Old and S. B. Primrose, Principles of Gene Manipulation, Blackwell Scientific Publications 59-88 (1980).
D. M. Glover, Genetic Engineering Cloning DNA, Chapman and Hall 36-48 (1980).
T. Maniatis et al., Molecular Cloning, A Laboratory Manual, Cold Spring Harbor iii., iv., 211-246; 309-361; 403-433 (1982).
Goodman et al., Methods in Enzymology, Academic Press 68:75-90 (1979).
A. J. Maxam and W. Gilbert, "A new method for sequencing DNA", Proc. Natl. Acad. Sci. USA 74(2):560-564 (1977).
L. Guarente et al., "Improved Met hods for Maximizing Expression of a Cloned Gene: a Bacterium That Synthesizes Rabbit .beta.-Globin", Cell 20:543-553 (1980).
Maxam et al, Methods in Enzymology, Academic Press 65:499-559 (1980).
R. Dulbecco, "Contributions of Microbiology to Eucaryotic Cell Biology: New Directions for Microbiology", Microbiological Reviews 43(4):443-452 (1979).
S. D. Ehrlich and V. Sgaramella, "Barriers to the heterospecific gene expression among prokaryotes", TIBS Nov. 1978:259-261.
R. W. Old and S. B. Primrose, "Principles of Gene Manipulation: An Introduction to Genetic Engineering", Studies in Microbiology vol. 2, pp. 104-105 (1981).
Ernst-L. Winnacker, "Gene und Klone", Vevlag Chemie, pp. 257-258 (1984). (German language document).
Beppu, et al., "Cloning of cDNA of calf prorennin in E. coli" Proceedings IV Int. Fermentation (1980), p. 179, F-21-5(L).
Foltman, B., "The Biochemistry of Prorennin & Rennin", Milk Proteins, 2:217-255 (1971).
Foltman, B., "Prochymosin & Chymosin", Methods Enzymol. 19:421-436 (1970).
Nishimori, et al. "Cloning of Prorennin Structured Genes", Abs. of AM of Japan Ag. Chem. Society (1981), cf. PTO-1019.
Moir, D., et al. Molecular Cloning and Characterization of double-stranded cDNA coding for bovine chymosin, Gene 19:127-138 (1982).
Chang, et al, "Phenotypic expression in E. coli of a DNA Sequence coding for mouse dihydrofolate reductase", Nature 275:617-624 (1978).
Goeddel, D. V., et al., "Direct expression in Escherichia coli of a DNA sequence coding for human growth hormone," Nature 281:544-548 (1979).
Uchiyama, H., et al., "Purification of prorennin mRNA and its translation in Vitro," Agric. Biol. Chem. 44:1373-1381 (1980).
Nishimori, K., et al., "Cloning in Escherichia coli for the structural gene of prorennin, the precursor of calf milk-clotting enzyme rennin," J. Biochem. 90:901-904 (1981).
Nishimori, K., et al., "Nucleotide sequence of calf prorennin cDNA cloned in Escherichia coli," J. Biochem. 91:1085-1088 (1982).
Harris, T. J. R., et al., "Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin," Nuc. Acids Res. 10:2177-2187 (1982).
MacDonald, et al., "Structure of a family of rat amylase genes," Nature 287:117-122 (1980).
Ehring, et al., "In vitro and in vivo products of E. coli lactose permease gene are identical," Nature 283:537-540.
Williamson, et al., "Isolation of the structural gene for alcohol dehydrogenase by genetic complementation in yeast," Nature 283:214-216 (1980).
Nishimori, et al., "Cloning of the Structural Gene of Prorennin," Abs of AM of the Japan Ag. Chem. Society, 1980, p. 408.
Hitzeman, et al., "Expression of a human gene for interferon in yeast," Nature 293:717-722 (1981).
Houghton, et al., "The amino-terminal sequence of human fibroblast interferon as deduced from reverse transcripts obtained using synthetic oligonucleotide primers," Nucl. Acids Res. 8:1913-1931 (1980).
Martin, et al., "Kinetic Studies on the Action of Mucor pusillus, Mucor miehi Acid Proteases and Chymosins A and B on a Synthetic Chromophoric Hexapeptide," Biophys. Acta. 612:410-420 (1980).
Collin, et al., "Immunological identification of milk clotting enzymes," J. Dairy Research 49:221-230 (1982).
Martin, et al., "Qualitative and quantitative analysis of commercial calf and bovine rennets," Neth. Milk Dairy J., 35:370-373 (1981).
Prager, "Differentiation of Rennet from Other Milk-Clotting Enzymes by Polyacrylamide Gel Electrophoresis," J. AOAC 60:1372-1374 (1977).
O'Leary et al., "A method for the quantitative analysis of the enzyme complement of commercial rennents" J. Dairy Research 41:381-387 (1974).
Righetti, et al., "Isoelectric focusing of milk-clotting enzymes," J. Dairy Research 44:69-72 (1977).
Matheson, et al., "The Immunochemical Determination of Chymosin Activity in Cheese," N. Z. J. Dairy Sci. and Tech. 15:33-41 (1981).
Vigyazo, et al., "Comparative Investigations into the Action of Chymosin and a Microbial Milk-Clotting Enzyme Preparation on Some Milk Proteins--I. Decomposition of .alpha..sub.s Casein," Acta Alimentaria 9:383-390 (1980).
Kay, et al., Neth. Milk Dairy J. 35:281-286 (1981).
Ernstrom, et al., Fund. of Dairy Chem. pp. 103, 111, 118-124, 604-608, 662-718 and 753-771.
Foltman, et al., "The Primary Structure of Calf Chymosin," J. Biol. Chem. 254:8447-8456 (1979).
Nishimori, et al., "Expression of cloned calf prochymosin gene sequence in Escherichia coli," Gene 19:337-344 (1982).
Emtage, et al., "Synthesis of calf prochymosin (prorennin) in Escherichia coli," Proc. Natl. Acad. Sci. 80:3671 (1983).
Mellor, et al., "Efficient synthesis of enzymatically active calf chymosin in Saccharomyces cerevisiae, " Gene 24:1 (1983).
Bu/ chel, et al., "Sequence of the lactose permease gene," Nature 283: 541-545 (1980).
Guarente, et al., "A Technique for Expressing Eukaryotic Genes in Bacteria", Science 209:1428-1430 (1980).
Talmadge, et al., "Bacteria mature preproinsulin to proinsulin", Proc. Natl. Acad. Sci. USA 77:3988-3992 (1980).
Foltman, et al., "The complete amino acid sequence of prochymosin", Proc. Natl. Acad. Sci. USA 74:2321-2324 (1977).

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

Processes for producing pre-prorennin, prorennin and rennin does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Processes for producing pre-prorennin, prorennin and rennin, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Processes for producing pre-prorennin, prorennin and rennin will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1412385

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