Search PubMed⌕ Search

Biomedical subjects

J Mizon

Publications and source records attributed to J Mizon.

At least 73 records · Page 4Linked to original sources

Histones from gonads of the star-fish Asterias rubens.

1. Histones were isolated from gonads of the star-fish Asterias rubens and characterized by their amino acid composition and their electrophoretic migration. 2. Comparative studies with calf thymus homologous histones show the highly conservative structure of the histones H3 and H4, and the variability of the other histones namely H1 and H2B.

Amino Acids↗

[The fate of alpha and epsilon lysine amino groups in rat liver in vitro (author's transl)].

The fate of alpha and epsilon lysine amino groups has been explored in rat liver homogenate by means of L-lysine labelled selectively in the two positions. alpha-15NH2 and epsilon-15NH2 are rapidly incorporated into the amino group of glutamic acid and it seems at first that both transaminations occur simultaneously. But the reversible transfer of the amino group between alpha-aminoadipic acid and glutamic acid, determined by means of labelled alpha-aminoadipic acid, proceeds swiftly, and the incorporation of alpha-15NH2 from the corresponding labelled lysine in glutamic acid may be easily explained by epsilon-transamination and saccharopine formation. The direct transamination of the alpha-amino group of L-lysine is most improbable and might be limited to some microorganisms and to epsilon-N-substituted lysine derivatives.

2-Aminoadipic Acid↗

[Properties of histones on hydrophobic chromatography].

The hydrophobic chromatography on alkylated Sepharose allows to separate the histones into three groups which exhibit an increasing affinity for the support HI less than H2A-H2B less than H3-H4. In this fractionation procedure, the behaviour of the histones taken separately or pair-associated, is discussed in relation with the ability of these proteins to complex each other in vitro and in vivo.

Adsorption↗

Functional and immunoreactive alpha 1 proteinase inhibitor in bronchoalveolar lavages: methodological studies.

The functional activity of alpha 1 proteinase inhibitor (alpha 1PI) in bronchoalveolar lavages (BAL) was determined with an automated method, using its inhibitory capacity against porcine pancreatic elastase. Immunoreactive alpha 1PI was measured by immunonephelometry-laser (INL). These two methods may generally be applied on unconcentrated samples. Precision and accuracy of both methods are studied. INL was preferably used to electroimmunodiffusion (EID) because it gave unchanged values after alpha 1PI had reacted with proteases. In BAL, for some specimens, the alpha 1PI content evaluated by EID was underestimated with respect to its measurement by INL. The degree of underestimation is related to the presence of non-functional forms of alpha 1PI.

Blood Proteins↗