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F Schoentgen

Publications and source records attributed to F Schoentgen.

34 records · Page 2Linked to original sources
PubMed1986

Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.

The complete amino acid sequence (458 amino acid residues) of human group-specific component 2 (Gc2) protein was determined. Computer analyses established a three-fold internal homology of Gc2 protein as well as an extensive homology between the overall structures of Gc2 protein, human serum albumin and human alpha-fetoprotein.

Amino Acid Sequence↗
PubMed1984

Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins.

The complete amino acid sequence (703 amino acid residues) of human lactotransferrin has been determined. The location of the disulfide bridges has also been investigated. Computer analysis established internal homology of the two domains (residues 1-338 and residues 339-703). Each domain contains a single iron-binding site and a single glycosylation site (asparagine residues 137 and 490) located in homologous positions. Prediction of the secondary structure of the two homologous moieties of human lactotransferrin has also been performed. The present results allowed a series of comparisons to be made with human serum transferrin and hen ovotransferrin.

Amino Acid Sequence↗
PubMed1984

Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes.

The complete sequence of 129 amino acids has been determined for one of three closely related lysozymes c purified from cow stomach mucosa. The sequence differs from those known for 17 other lysozymes c at 39-60 positions, at one of which there has been a deletion of 1 amino acid. The glutamate replacement at position 101 and the deletion of proline at position 102 eliminate the aspartyl-prolyl bond that is present between these positions in all other mammalian lysozymes c tested. This bond appears to be the most acid-sensitive one in such lysozymes at physiological temperature. Of the 40 positions previously found to be invariant among lysozymes c, only one has undergone substitution in the cow lineage. This modest number of changes at novel positions is consistent with the inference, based on tree analysis and antigenic comparisons, that the tempo of evolutionary change in the cow lysozyme lineage has not been radically different from that in other lysozyme c lineages. The mutations responsible for the distinctive catalytic properties and stability of cow lysozyme c could be a minor fraction of the total that have been fixed in the cow lineage.

Amino Acid Sequence↗
PubMed1982

Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose-type lysozyme.

The complete amino acid sequence (185 amino acid residues) of the good-type lysozyme from the egg white of ostrich (Struthio camelus) has been determined from the study of tryptic and Staphylococcus aureus V8 protease peptides as well as of CNBr and BNPS-skatole fragments. A slight sequence homology between the goose-type and chicken-type lysozymes has been observed.

Amino Acid Sequence↗
PubMed1976

Amino acid sequence and immunological properties of chalchalaca egg white lysozyme.

The amino acid sequence of lysozyme c from chachalaca egg white was determined. Like other bird lysozymes c, that of the chachalaca has 129 amino acid residues. It differs from other avian lysozymes c by 2 to 31 amino acid substitutions as well as by being devoid of phenylalanine. It contains substitutions at 9 positions which are invariant in the other 7 bird lysozymes of known sequence. Although the chachalaca is classified zoologically in the order Galliformes, which includes chickens and other pheasant-like birds, its lysozyme differs more from those of pheasant-like birds than do the lysozymes c of ducks. Phylogenetic analysis of the sequence comparisons confirms that the lineage leading to chachalaca lysozyme c separated from that leading to other galliform lysozymes c before the duck lysozyme c lineage did. This indicates a contrast between protein evolution and evolution at the organismal level. Immunological comparison of chachalaca lysozyme c with other lysozymes of known sequence provides further support for the proposal that immunological cross-reactivity is strongly dependent on degree of sequence resemblance among bird lysozymes.

Amino Acid Sequence↗
PubMed1970

Purification of soluble murine transplantation antigens by isoelectric focusing.

Hydrosoluble transplantation antigens were prepared from membranes and microsomes of C(3)H mice (BP8 tumoral cells) and purified by isoelectric focusing. A biologically active fraction which seems homogenous by acrylamide gel electrophoresis was characterized: it specifically inhibits anti C(3)H hemagglutinin antibodies and provokes a highly significant prolongation of skin graft.

Journal Article↗
PubMedDate not supplied

Amino acid sequence and some ligand binding properties of fatty acid-binding protein from bovine brain.

A fatty acid-binding protein (FABP) from the cytosol of bovine brain was purified by Sephadex G-75 filtration and electrofocusing. The purified protein migrated as a single protein band in 15% polyacrylamide gel electrophoresis with an apparent molecular mass of 14.7 kDa. To ascertain that the purified protein was a FABP, it was submitted to fatty acid-binding tests. Oleic and palmitic acids bound to brain FABP but this was not the case for palmitoyl CoA. By Scatchard analysis the ligand binding values were: Kd = 0.28 microM, Bmax (mol/mol) = 0.6 for oleic acid and Kd = 0.8 microM, Bmax (mol/mol) = 2.1 for palmitic acid. The complete amino acid sequence of the brain FABP was determined and a microheterogeneity was observed. Sequence comparison with other FABPs of known sequence and the observed microheterogeneity demonstrated the presence in brain of several homologous FABPs closely related to heart FABP.

Amino Acid Sequence↗