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Biomedical subjects

G Biserte

Publications and source records attributed to G Biserte.

At least 109 records · Page 6Linked to original sources
PubMed1975

Immunochemical and biochemical study of a human Fcmu-like fragment (mu-chain disease).

An abnormal protein, from a petient with mu-chain disease has been studied: protein BUR. It is devoid of the F (ab'')2 mu fragment; molecular weight determinations and immunological data identify the protein as a F(c) 5 mu fragment. Similarly, carbohydrate determinations and proteolysis experiments relate it to a Fcmu fragment. Nevertheless, the protein, which tontains J-chain, lacks the entire covalently bonded structure of the F (c)5mu fragment. C-terminal analysis shows a tyrosine residue identical to the C-terminal amino acid of mu-chains. Sequence of the N-terminal region determined for 15 residues shows identity with sequence 338-352 and sequence 333-347 of two entire mu-chains previously studied. The relation of BUR to other heavy chain disease proteins is discussed.

Amino Acid Sequence↗
PubMed1975

Isolation and characterization of the cyanogen bromide fragments of lobster arginine kinase (homarus vulgaris).

Arginine kinase was aminoethylated in order to block the five free thiol groups on the native enzyme, and then submitted to BrCN cleavage. The BrCN resulting peptides were soluble in propionic acid (10 percent) and subsequently submitted to gel-filtration. The large polypeptide subfractions were citraconylated and resubmitted to differnt gelchromatographies, whereas the short peptide subfractions were submitted to preparative paper electrochromatographies. Eight peptides of 2, 11, 17, 25, 61, 82, 86 and 132 amino acid residues were isolated, one of which is the overlapping of two peptides. The amino acid composition and the end group of all the isolated peptides were established. The short peptides (2, 11 and 17 residues) were sequenced. All peptides possess homoserine at C-terminal position because one methionyl residue is situated at the C-terminal position in the native protein. The polypeptide with 132 residues possessed N-acetylated residue at N-terminal position: therefore this polypeptide is located at the N-terminal position in the protein. The sum and account of each amino acid of the seven isolated peptides were compared to those of the intact protein: the sum of the seven peptides is 331 amino acid residues, whereas the whole protein contains 342 residues. The molecular weight of arginine kinase is revised and calculated on the basis of the present results (37, 687).

Amino Acid Sequence↗
PubMed1975

[Natural history of molecular pathology].

The author recalls the main stages of biosynthesis of proteins based on molecular pathology : transcription of DNA into messenger RNA, the genetic code, translation of protein molecules and regulation of their synthesis. Examples are then given of qualitative and quantitative disturbances. Qualitative disturbances with synthesis of abnormal proteins, or protein diseases of protein structure, together with their consequences. Quantitative disorders, with modified synthesis of normal proteins, result very often from abnormalities of structural genes, but also from abnormalities of transcription or translation. The author considers, in conclusion, pathological situations based on molecular abnormalities for mutations occur at random and it may be possible to correct them by genetic manipulation.

Amino Acid Sequence↗
PubMed1975

[Report on the study of hyaluronic acid in the diagnosis of pleural mesotheliomas: study of 100 hyaluronic acid rich effusions].

Hyaluronic acid was measured in 1580 pleural effusions. We report 100 cases of hyaluronate-rich pleural fluids. Correlations betueen clinical, radiological and histological diagnosis of mesothelioma and the characterization of hyaluronate are discussed. These data suggest the possibility of a biochemical approach for the diagnosis of pleural malignant tumours.

Asbestosis↗