Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
2008-01-29
2008-01-29
Slobodyansky, Elizabeth (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
C435S252300, C435S254110, C435S320100, C435S325000, C536S023200
Reexamination Certificate
active
10399026
ABSTRACT:
The present invention relates to a nucleic acid molecule comprising a nucleotide sequence as set forth in SEQ ID Nos. 1 or 20 or having at least 55% sequence identify therewith and/or capable of hybridising under medium stringency conditions to the complementary sequence of SEQ ID Nos. 1 or 20, or the complementary sequence of said sequences, wherein said nucleotide sequence encodes or is complementary to a sequence which encodes a heat labile alkaline phosphatase and to a recombinant heat labile alkaline comprising: (a) all or a significant part of an amino acid sequence as shown in SEQ ID No. 2; or (b) all or a significant part of an amino acid sequence which has at least 60% sequence identify with SEQ ID No. 2 as well as methods for the manufacture thereof.1kAYWNKDAQDALDKQLGIKLREKQAKNVIFFLGDGMSLSTVTAARIYKGG 5ReRP6:1751LTGKFEREKISWEEFDFAALSKTYNTDKQAYLTGVKTNQGV Active site101IGLDANTVRTNCSYQLDESLFTYSIAHWFQEAGRSTGVVTSTRVTHATPA151GTYAHVADRDWENDSDVVHDREDPEICDDIAEQLVFREPGKNFKVIMGGG 5ReRP6:26201RRGFFPEEALDIEDGIPGEREDGKHLITDWLDDKASQGATASYVWNRDDL H23:30251LAVDIRNTDYLMGLFSYTHLDTVLTRDAEMDPTLPEMTKVAIEMLTKDEN301GFFLLVEGGRIDHMHHANQIRQSLAETLDMEEAVSMALSMTDPEETIILV351TADHGHTLTITGYADRNTDILDFAGISDLDDRRYTILDYGSGPGYHITED401GKRYEPTEEDLKDINFRYASAAPKHSVTHDGTDVGIWVNGPFAHLFTGVY H23:18451EENYIPHALAYAACVGTGRTFCDEK *
REFERENCES:
patent: 5741676 (1998-04-01), Fuller
patent: 5756285 (1998-05-01), Fuller
patent: WO 00/34476 (2000-06-01), None
Nilsen et al. (Jul. 2001) Comparative Biochemistry and Physiology Part B, vol. 129, pp. 853-861.
Kobori, H., et al., “Heat-labile Alkaline Phosphatase from Antarctic Bacteria: Rapid 5′ End-Labeling of Nucleic Acids,”Proc. Natl. Acad. Sci. USA 81:6691-6695, Nov. 1984.
Rina, M., et al., “Alkaline Phosphatase from the Antarctic Strain TAB5. Properties and Psychronphilic Adaptations,”Eur J Biochem. 267(4):1230-8, Feb. 2000.
Ásgeirsson et al., “Alkaline phosphatase from Atlantic Cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures.”Comp. Biochem. Physiol. 110B(2):315-329 (1995).
De Prada et al., “Purification and Characterization of Two Extracellular Alkaline Phosphatases from a PsycrophilicArthrobacterIsolate.”Appl. Env. Microbiol63(7):2928-2931 (Jul. 1997).
Lee and Chuang, “Characterization of different molecular forms of alkaline phosphatase in the hepatopancreas from shrimpPenaeus monodon(Crustacea: Decapoda).”Comp. Biochem. Physiol. 99B(4):845-850 (1991).
Olsen et al., “Alkaline phosphatase from the hepatopancreas of shrimp (pandalus borealis): a dimeric enzyme with catalytically active subunits.”Biochem. Physiol. 99B(4):755-761 (1991).
Olsen et al., “Recovery of Enzymes from Shrimp Waste.”Process Biochem. 25:67-68 (Apr. 1990).
Shandilya and Chatterjee, “An engineered thermosensitive alkaline phosphate for dephosphorylating DNA.”Focus17(3):93-95 (1995).
Whitmore and Goldberg. “Trout intestinal alkaline phosphatases. II. The effect of temperature upon enzymatic activity in vitro and in vivo.”J. Exp. Zool. 182(1):59-68 (1972).
Lanes Olav
Nilsen Inge
Överbö Kersti
Biotec Pharmacon ASA
Seed IP Law Group PLLC
Slobodyansky Elizabeth
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