Shrimp alkaline phosphatase

Details Shrimp alkaline phosphatase Shrimp alkaline phosphatase

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

07323325

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).

Affiliated with

Also associated with

Rating

Shrimp alkaline phosphatase does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Shrimp alkaline phosphatase, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Shrimp alkaline phosphatase will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-2762385