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Biomedical subjects

S Magnusson

Publications and source records attributed to S Magnusson.

At least 73 records · Page 4Linked to original sources
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↗
PubMed1977

The influence of the bony pelvis in persistent occiput posterior position.

Roentgenologic pelvimetry has been performed in 68 consecutive cases of occiput posterior position. The results point to an influence from a transverse narrowing of the pelvis or a tendency towards large dimensions. In many cases, however, no clear correlation to pelvic dimensions is found. A significant difference exists in the rate of obstetrical complications between nulliparous and parous women. The reasons for this and for the persistent OP position are discussed.

Female↗
PubMed1977

The effect of oxytocin on hypertonic saline abortion.

Oxytocin was infused in 22 randomly selected pregnant women after extraamniotic hypertonic saline instillation. In another 24 pregnant women no oxytocin was infused at midtrimester abortion. There was no difference between the two groups in mean time from saline injection to expulsion of the fetus.

Abortion, Induced↗
PubMed1976

Hirudin.

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Amino Acid Sequence↗
PubMed1975

Amino-acid sequence of activation cleavage site in plasminogen: homology with "pro" part of prothrombin.

A 38-residue fragment is isolated from carboxymethylated plasminogen. Residues 29-38 have the same sequence as the amino-terminal end of the light chain of plasmin. The sequence 1-28 is therefore the sequence of the carboxyl-terminal end of the heavy chain and contains the specific sequence at which urokinase (EC 3.4.99.26) and other plasminogen-activating serine proteases split. Two of the five carboxymethyl-cysteine residues in the isolated fragment are situated close to the cleavage site and the fragment is not itself a substrate for plasminogen-activators. Residues 1-11 show extensive sequence homology with residues 137-147 and 242-252 in prothrombin, which are located in corresponding regions of the two internally homologous 83-residue structures in the non-thrombin part of the molecule, indicating that such structures may be a common feature of the non-protease part of the larger serine protease zymogens.

Amino Acid Sequence↗
PubMed1971

[Nodular fasciitis].

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Diagnosis, Differential↗