PubMed Health⌕ Search

Biomedical subjects

L Sottrup-Jensen

Publications and source records attributed to L Sottrup-Jensen.

At least 127 records · Page 7Linked to original sources
PubMed1981

Adsorption to fibrin of native fragments of known primary structure from human plasminogen.

Limited proteolysis of native Glu-plasminogen with pancreatic elastase produced three major fragments, K1+2#3, K4, K5-light chain (miniplasminogen). Fibrin-binding was determined by clotting fibrinogen in the presence of 125I-labelled fragments and measuring 125I in the washed fibrin and in the supernatant. Of the fragments miniplasminogen showed the highest fibrin-binding, the strength of which was intermediate between those of Glu-plasminogen and Lys-plasminogen. The fibrin-binding of all three fragments was decreased by 6-aminohexanoic acid or tranexamic acid. This decrease was most pronounced with K1+2+3. The fibrin-binding of K1+2+3, but not that of K4 and miniplasminogen was decreased by alpha 2-antiplasmin. The fibrin-binding of K1+2+3 and mini-plasminogen was lower in a plasma clot than in a purified fibrin clot. Our results indicate that each of the three fragments can bind to fibrin. They confirm that an alpha 2-antiplasmin-binding site is located on K1+2+3. Furthermore two of the fragments, namely K4 and K1+2+3 contain lysine-binding site(s).

Binding Sites↗
PubMed1980

The complete amino-acid sequence of elongation factor Tu from Escherichia coli.

The complete primary structure of elongation factor Tu from Escherichia coli has been elucidated. The protein, which is a mixture of two gene products, consists of a single polypeptide chain of 393 residues. After tryptic digestion of S-carboxymethylated protein, 50 tryptic peptides were isolated covering the complete protein chain. Their alignment was established with overlapping peptides obtained by chemical cleavage with cyanogen bromide and subsequent enzymic subdigestion with Staphylococcus aureus protease, chymotrypsin, elastase and thermolysin. Peptides were sequenced by manual dansyl-Edman and direct Edman degradation procedures. The N-terminal amino acid of EF-Tu is serine and is N-acetylated. The lysine residue at positon 56, in the polypeptide chain is partly methylated. The C-terminal residue is a mixture of serine and glycine, and this was the only heterogeneity found in the EF-Tu preparation used in this study.

Amino Acid Sequence↗
PubMed1978

The N-terminal sequences of blood coagulation factor X1 and X2 light chains. Mass-spectrometric identification of twelve residues of gamma-carboxyglutamic acid in their vitamin K-dependent domains.

Peptides (residues 1-42) (bovine prothrombin numbering) from bovine Factor X1 and X2 have been separately purified and digested before mass-spectrometric sequence assignment and identification of gamma-carboxyglutamic acid. N-terminal sequence was found to be identical, and 12 residues of gamma-carboxyglutamic acid were unambiguously identified. The new data give conclusive evidence for the N-terminal primary structure of bovine Factor X and extend present knowledge to show (i) unambiguous assignment of gamma-carboxyglutamic acid residues, including a previously unreported residue of gamma-carboxyglutamic acid at position 40 in both Factor X1 and X2, (ii) the physical difference between Factors X1 and X2 is not due to either different amino acid sequences or different gamma-carboxyglutamic acid contents of the N-terminal 42 residues.

1-Carboxyglutamic Acid↗