Human plasminogen activator variants having amino acids 37-42 su

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435212, 4352402, 4353201, 536 232, C12N 500, C12N 1500, C12N 1558, A61K 37547

Patent

active

054078199

ABSTRACT:
A TPA variant with replacement of amino acids is provided. In a typical embodiment, the variant has an amino acid sequence with replacement of the amino acid group consisting of asparagine at the 37th position, serine at the 38th position, glycine at the 39th position, arginine at the 40th position, alanine at the 41st position, and glutamine at the 42nd position from the N-terminus of the amino acid sequence of mature human tissue plasminogen activator.

REFERENCES:
"Cloning and Expression of Human Tissue-Type Plasminogen Activator cDNA in E. coli", D. Pennica, et al., Nature, vol. 301, Jan. 20, 1983, pp. 214-221.
"Recombinant Tissue Plasminogen Activator: A Brief Review", E. B. Grossbard, Pharmaceutical Research, vol. 4, No. 5, 1987, pp. 375-378.
"Catabolism of Human Tissue Plasminogen Activator in Mice", H. E. Fuchs, et al., Blood. vol. 65, No. 3, Mar. 1985, pp. 539-544.
"Coronary Thrombolysis in Dogs with Intravenously Administered Human Prourokinase", D. Collen, et al., Circulation, vol. 72, No. 2, Aug. 1985, pp. 384-388.
"A Tissue-Type Plasminogen Activator Mutant with Prolonged Clearance in Vivo", M. J. Browne, et al., The Journal of Biological Chemistry, vol. 263, No. 4, Feb. 5, 1988, pp. 1599-1602.
"Isolation, Identification and Pharmacokinetic Properties of Human Tissue-type Plasminogen activator Species: Possible Localisation of a Clearance Recognition Site", I. Dodd, et al. Thrombosis and Haemostasis, vol. 59, No. 3, 1988, pp. 523-528.
"Structure-Function Analysis with Tissue-Type Plasminogen Activator", N. K. Kalyan, et al., The Journal of Biological Chemistry, vol. 263, No. 8, Mar. 15, 1988, pp. 3971-3978.
"Variants of Human Tissue-type Plasminogen Activator", G. R. Lansen, et al., The Journal of Biological Chemistry, vol. 263, No. 2, Jan. 15, 1988, pp. 1023-1029.
"Functional Effects of Asparagine-linked Oligosaccharide on Natural and Variant Human Tissue-type Plasminogen Activator", L. Hansen, et al., The Journal of Biological Chemistry, vol. 263, No. 30, Oct. 25, 1988, pp. 15713-15719.
"Pharmacokinetics and Thrombolytic Properties of Deletion Mutants of Human Tissue-Type Plasminogen Activator in Rabbits", D. Collen, et al., Blood, vol. 71, Jan., 1988, pp. 216-219.
"On the Interaction of the Finger and the Kringle-2 Domain of Tissue-type Plasminogen Activator with Fabrin", A. J. Zonneveld, et al., The Journal of Biological Chemistry, vol. 261, No. 30, Oct. 25, 1986, 1983, pp. 14214-14218.
"Continuous Production of Erythropoietin by an Established Human Renal Carcinoma Cell Line: Development of the Cell Line", J. B. Sherwood, et al., Proc. Natl. Acad. Sci. USA, vol. 83, Jan., 1986, pp. 165-169.
"Biological and Functional Characterization of Human Tissue-Type Plasminogen Activator Variants With Mutagenized Kringle Domains", Collen et al, The Journal of Biological Chemistry, vol. 265, No. 21, Jul. 25, 1990, pp. 12184-12191.

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

Human plasminogen activator variants having amino acids 37-42 su does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Human plasminogen activator variants having amino acids 37-42 su, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Human plasminogen activator variants having amino acids 37-42 su will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-66295

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