Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
31
1
2

Year Published

2002
2002
2013
2013

Publication Types

Select...
4
2

Relationship

0
6

Authors

Journals

citations
Cited by 45 publications
(35 citation statements)
references
References 14 publications
1
31
1
2
Order By: Relevance
“…The site of binding of the TN8.2 peptide to the BDDrFVIII molecule was determined by peptide blot screening of both Achro-K digested fragments of BDDrFVIII and synthetic peptides derived from the BDDrFVIII sequence. The TN8.2 peptide binds BDDrFVIII in the C2 domain, within the light chain (Sandberg et al, 2001). Because of this specificity, free light chain would be expected to bind to the TN8.2 Sepharose, but differential binding affinity in relation to BDDrFVIII could arise from subtle folding differences arising from the lack of a heavy chain partner.…”
Section: Characterization Of Tn82 Peptide -Bddrfviii Interactionmentioning
confidence: 99%
See 2 more Smart Citations
“…The site of binding of the TN8.2 peptide to the BDDrFVIII molecule was determined by peptide blot screening of both Achro-K digested fragments of BDDrFVIII and synthetic peptides derived from the BDDrFVIII sequence. The TN8.2 peptide binds BDDrFVIII in the C2 domain, within the light chain (Sandberg et al, 2001). Because of this specificity, free light chain would be expected to bind to the TN8.2 Sepharose, but differential binding affinity in relation to BDDrFVIII could arise from subtle folding differences arising from the lack of a heavy chain partner.…”
Section: Characterization Of Tn82 Peptide -Bddrfviii Interactionmentioning
confidence: 99%
“…BDDrFVIII is expressed as a mixture of isoforms arising from differential processing of the heavy chain carboxyl terminus and incomplete cleavage of the translation fusion gene product (Sandberg et al, 2001). The BDDrFVIII isoforms captured and recovered using either TN8.2 Sepharose or Mab Sepharose steps are equivalent, as evaluated by silver-stained and anti-FVIII SDS-PAGE analysis, and RP-HPLC for all in-process pools after the TN8.2 step (data not shown).…”
Section: Tn82 Sepharose Step Performancementioning
confidence: 99%
See 1 more Smart Citation
“…The factor VIII gene cloned in 1984, is 186 kb with 26 exons, a cDNA of 7.05 kb, that encodes a polypeptide of 2351 amino acids that has six domains. 6,7 The large size of the gene for FVIII provides a challenge for gene transfer, as many viral vectors cannot accommodate the gene. However, by removing the B-domain the cDNA is reduced to 4.35 kb, a reduction of approximately 40% reducing the challenge of packaging 7 and removing a region that requires complicated post-translation modification.…”
Section: Transgenementioning
confidence: 99%
“…6,7 The large size of the gene for FVIII provides a challenge for gene transfer, as many viral vectors cannot accommodate the gene. However, by removing the B-domain the cDNA is reduced to 4.35 kb, a reduction of approximately 40% reducing the challenge of packaging 7 and removing a region that requires complicated post-translation modification. Infusion of a commercially available B-domain deleted (BDD) FVIII protein is associated with hemostatic efficacy despite the significant size reduction.…”
Section: Transgenementioning
confidence: 99%