Characterization of the Polypeptide Composition of Human Factor VIII

C and the Nucleotide Sequence and Expression of the Human Kidney cDNA

M. A. Truett, R. Blacher, R. L. Burke, D. Caput, C. Chu, D. Dina, K. Hartog, C. H. Kuo, F. R. Masiarz, J. P. Merryweather, R. Najarian, C. Pachl, S. J. Potter, J. Puma, M. Quiroga, L. B. Rall, A. Randolph, M. S. Urdea, P. Valenzuela, H. H. Dahl & 4 otros J. Favalaro, J. Hansen, O. Nordfang, M. Ezban

Resultado de la investigación: Article

74 Citas (Scopus)

Resumen

Human coagulation factor VIII:C has been purified approximately 5000-fold from commercial preparations with an average activity yield of 35%. Proteins of 92 kD and 77–80 kD enriched during purification are precipitated by a human serum polyclonal antibody which inhibits factor VIII:C activity. Evidence suggests that these polypeptides are linked by a calcium ion bridge. Partial amino acid sequence information from these proteins has been obtained from the intact polypeptides and from products of digestion with thrombin, endoproteinase lysC, or trypsin after citraconylation. An oligonucleotide probe designed from one of the amino acid sequences was used to isolate a partial genomic clone from a human 4X chromosome library in bacteriophage λ. The genomic segment was used to isolate two cDNA molecules encompassing the entire human kidney factor VIII:C mRNA. Biologically active factor VIII:C has been produced in a mammalian cell line utilizing a complete cDNA construction.

Idioma originalEnglish
Páginas (desde-hasta)333-349
Número de páginas17
PublicaciónDNA
Volumen4
N.º5
DOI
EstadoPublished - 1985

Huella dactilar

Factor VIII
Nucleotides
Complementary DNA
Kidney
Peptides
Amino Acid Sequence
Chemical analysis
Oligonucleotide Probes
Human Chromosomes
Amino Acids
Thrombin
Bacteriophages
Trypsin
Digestion
Proteins
Chromosomes
Clone Cells
Ions
Calcium
Purification

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

Citar esto

Truett, M. A. ; Blacher, R. ; Burke, R. L. ; Caput, D. ; Chu, C. ; Dina, D. ; Hartog, K. ; Kuo, C. H. ; Masiarz, F. R. ; Merryweather, J. P. ; Najarian, R. ; Pachl, C. ; Potter, S. J. ; Puma, J. ; Quiroga, M. ; Rall, L. B. ; Randolph, A. ; Urdea, M. S. ; Valenzuela, P. ; Dahl, H. H. ; Favalaro, J. ; Hansen, J. ; Nordfang, O. ; Ezban, M. / Characterization of the Polypeptide Composition of Human Factor VIII : C and the Nucleotide Sequence and Expression of the Human Kidney cDNA. En: DNA. 1985 ; Vol. 4, N.º 5. pp. 333-349.
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title = "Characterization of the Polypeptide Composition of Human Factor VIII: C and the Nucleotide Sequence and Expression of the Human Kidney cDNA",
abstract = "Human coagulation factor VIII:C has been purified approximately 5000-fold from commercial preparations with an average activity yield of 35{\%}. Proteins of 92 kD and 77–80 kD enriched during purification are precipitated by a human serum polyclonal antibody which inhibits factor VIII:C activity. Evidence suggests that these polypeptides are linked by a calcium ion bridge. Partial amino acid sequence information from these proteins has been obtained from the intact polypeptides and from products of digestion with thrombin, endoproteinase lysC, or trypsin after citraconylation. An oligonucleotide probe designed from one of the amino acid sequences was used to isolate a partial genomic clone from a human 4X chromosome library in bacteriophage λ. The genomic segment was used to isolate two cDNA molecules encompassing the entire human kidney factor VIII:C mRNA. Biologically active factor VIII:C has been produced in a mammalian cell line utilizing a complete cDNA construction.",
author = "Truett, {M. A.} and R. Blacher and Burke, {R. L.} and D. Caput and C. Chu and D. Dina and K. Hartog and Kuo, {C. H.} and Masiarz, {F. R.} and Merryweather, {J. P.} and R. Najarian and C. Pachl and Potter, {S. J.} and J. Puma and M. Quiroga and Rall, {L. B.} and A. Randolph and Urdea, {M. S.} and P. Valenzuela and Dahl, {H. H.} and J. Favalaro and J. Hansen and O. Nordfang and M. Ezban",
year = "1985",
doi = "10.1089/dna.1985.4.333",
language = "English",
volume = "4",
pages = "333--349",
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Truett, MA, Blacher, R, Burke, RL, Caput, D, Chu, C, Dina, D, Hartog, K, Kuo, CH, Masiarz, FR, Merryweather, JP, Najarian, R, Pachl, C, Potter, SJ, Puma, J, Quiroga, M, Rall, LB, Randolph, A, Urdea, MS, Valenzuela, P, Dahl, HH, Favalaro, J, Hansen, J, Nordfang, O & Ezban, M 1985, 'Characterization of the Polypeptide Composition of Human Factor VIII: C and the Nucleotide Sequence and Expression of the Human Kidney cDNA', DNA, vol. 4, n.º 5, pp. 333-349. https://doi.org/10.1089/dna.1985.4.333

Characterization of the Polypeptide Composition of Human Factor VIII : C and the Nucleotide Sequence and Expression of the Human Kidney cDNA. / Truett, M. A.; Blacher, R.; Burke, R. L.; Caput, D.; Chu, C.; Dina, D.; Hartog, K.; Kuo, C. H.; Masiarz, F. R.; Merryweather, J. P.; Najarian, R.; Pachl, C.; Potter, S. J.; Puma, J.; Quiroga, M.; Rall, L. B.; Randolph, A.; Urdea, M. S.; Valenzuela, P.; Dahl, H. H.; Favalaro, J.; Hansen, J.; Nordfang, O.; Ezban, M.

En: DNA, Vol. 4, N.º 5, 1985, p. 333-349.

Resultado de la investigación: Article

TY - JOUR

T1 - Characterization of the Polypeptide Composition of Human Factor VIII

T2 - C and the Nucleotide Sequence and Expression of the Human Kidney cDNA

AU - Truett, M. A.

AU - Blacher, R.

AU - Burke, R. L.

AU - Caput, D.

AU - Chu, C.

AU - Dina, D.

AU - Hartog, K.

AU - Kuo, C. H.

AU - Masiarz, F. R.

AU - Merryweather, J. P.

AU - Najarian, R.

AU - Pachl, C.

AU - Potter, S. J.

AU - Puma, J.

AU - Quiroga, M.

AU - Rall, L. B.

AU - Randolph, A.

AU - Urdea, M. S.

AU - Valenzuela, P.

AU - Dahl, H. H.

AU - Favalaro, J.

AU - Hansen, J.

AU - Nordfang, O.

AU - Ezban, M.

PY - 1985

Y1 - 1985

N2 - Human coagulation factor VIII:C has been purified approximately 5000-fold from commercial preparations with an average activity yield of 35%. Proteins of 92 kD and 77–80 kD enriched during purification are precipitated by a human serum polyclonal antibody which inhibits factor VIII:C activity. Evidence suggests that these polypeptides are linked by a calcium ion bridge. Partial amino acid sequence information from these proteins has been obtained from the intact polypeptides and from products of digestion with thrombin, endoproteinase lysC, or trypsin after citraconylation. An oligonucleotide probe designed from one of the amino acid sequences was used to isolate a partial genomic clone from a human 4X chromosome library in bacteriophage λ. The genomic segment was used to isolate two cDNA molecules encompassing the entire human kidney factor VIII:C mRNA. Biologically active factor VIII:C has been produced in a mammalian cell line utilizing a complete cDNA construction.

AB - Human coagulation factor VIII:C has been purified approximately 5000-fold from commercial preparations with an average activity yield of 35%. Proteins of 92 kD and 77–80 kD enriched during purification are precipitated by a human serum polyclonal antibody which inhibits factor VIII:C activity. Evidence suggests that these polypeptides are linked by a calcium ion bridge. Partial amino acid sequence information from these proteins has been obtained from the intact polypeptides and from products of digestion with thrombin, endoproteinase lysC, or trypsin after citraconylation. An oligonucleotide probe designed from one of the amino acid sequences was used to isolate a partial genomic clone from a human 4X chromosome library in bacteriophage λ. The genomic segment was used to isolate two cDNA molecules encompassing the entire human kidney factor VIII:C mRNA. Biologically active factor VIII:C has been produced in a mammalian cell line utilizing a complete cDNA construction.

UR - http://www.scopus.com/inward/record.url?scp=0022328654&partnerID=8YFLogxK

U2 - 10.1089/dna.1985.4.333

DO - 10.1089/dna.1985.4.333

M3 - Article

VL - 4

SP - 333

EP - 349

JO - DNA and Cell Biology

JF - DNA and Cell Biology

SN - 1044-5498

IS - 5

ER -