Late-onset fatal acute leucoencephalopathy in liver transplant recipient.
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Acute Disease↗
Biomedical subjects
E Ruban
Publications and source records attributed to E Ruban.
Is allopurinol beneficial in the prevention of renal ischaemia-reperfusion injury in the rat?: evaluation by near-infrared spectroscopy.
1. The role of allopurinol in the protection of kidney function following ischaemia-reperfusion injury has been investigated using the novel technique of near-infrared spectroscopy. 2. An in vivo model of rat kidney ischaemia was used, with the expected falls in blood and tissue oxygenation seen and confirmed by near-infrared spectroscopy. 3. Allopurinol infusion increased the rate of reperfusion of oxygenated blood seen in control rats (P < 0.05). 4. Allopurinol enhanced the rate of tissue oxygenation during early reperfusion (P < 0.01). 5. This study provides further evidence for the proposed benefits of allopurinol in ischaemia-reperfusion injury. Furthermore, the potential of near-infrared spectroscopy as a technique of value in interventional studies of this nature is confirmed.
Allopurinol↗
[Rule of antibody structure: the primary structure of a human monoclonal IgA1-immunoglobulin (myeloma protein Tro), I. Purification and characterization of the protein and its L- and H-chains (author's transl)].
Myeloma protein Tro was prepared from the serum of a myeloma patient by ammonium sulfate precipitation. It was purified by gel filtration and ion exchange chromatography or by Pevikon block electrophoresis. The purity of the preparation was tested by several electrophoretic or immunoelectrophoretic methods. L- and H-chains of the purified protein after reduction and alkylation were separated by gel chromatography. The protein and its L- and H-chains were characterized by amino acid analyses and end-group determinations.
Amino Acid Sequence↗
[Rule of antibody structure: the primary structure of a human monoclonal IgA1-immunoglobulin (myeloma protein Tro), II. Cleavage of the monomer IgA-molecule and the reduced and alkylated H- and L-chains by cyanogen bromide (author's transl)].
The monomer of myeloma protein Tro as well as the reduced and alkylated H- and L-chains were cleaved by cyanogen bromide. All cyanogen-bromide fragments were isolated and characterized by amino acid analyses, end-group and molecular weight determinations. The 4 smaller fragments of the 5 H-chain fragments were split with trypsin. The peptides were isolated and their primary structure was determined.
Amino Acid Sequence↗
[Rule of antibody structure: the primary structure of a human monoclonal IgA1-immunoglobulin (myeloma protein Tro), V. The arrangement of the tryptic peptides and a discussion of the complete primary structure of the H-chain (author's transl)].
This communication deals with the sequence work done with tryptic and chymotryptic peptides and some cyanogen bromide splitting products. With these peptides, and if necessary with their splitting peptides, the whole primary structure of the alpha1-H-chain of myeloma protein Tro is established. The position of the amides is determined by electrophoresis and digestion with aminopeptidase M. The alpha1-chain Tro comprises 475 amino acid residues. Because of its specific exchanges and deletions the variable part of alpha1-chain Tro belongs to subgroup III of variable parts of H-chains. The switch from the variable to the constant part occurs at position 119/120 and is analogous to other chains which have been sequenced up to now. The large number of cysteine residues in the alpha-chain which may influence the tertiary structure, especially in the hinge and the subsequent CH2-region, is noteworthy. Furthermore, myeloma protein Tro is compared with the other alpha1-chain Bur[5] sequenced in the meantime, and protein But[6], which is an IgA2 molecule of the allotype A2m(2).
Amino Acid Sequence↗
[The primary structure of a monoclonal IgA-immunoglobulin (IgA Tro.), II. The amino acid sequence of the H-chain, alpha-type, subgroup III; structure of the complete IgA-molecule (author's transl)].
The primary structure of a monoclonal human IgA-immunoglobulin has been determined. Sequence studies were carried out with the isolated L-chain [1], the isolated H-chain and with BrCN-fragments of the H-chain. Tryptic and chymotryptic peptides were prepared from the totally reduced and alkylated alpha-chain or from BrCN-fragments. Sequence work has been done with tryptic as well as chymotryptic peptides. The variable part comprised positions 1-119, the constant part residues 120-472. According to its homology with other variable parts alpha-chain Tro. clearly belongs to subgroup III of the H-chains. The constant part is composed of 3 homology regions (C1-C3) which originated from a common ancestor by repeated gene duplications early in evolution. Each homology region corresponds in its length and its sequence to the C-region of the L-chains. The hinge-region, which connects the C1- and the C2-region, originated from the C-terminal end of the C1-region by a twofold partial gene duplication comprising 8 amino acids. The C3-homology region is termined by an additional C-terminal piece of 18 residues. The alpha-chain 17 cysteine residues, 8 of which form the usual intrapeptidal loop S-S-bridges, and one the connection between the L- and H-chain. Two additional cysteine residues are located in the C1-region, and 5 more in the C2-region, forming intra- and inter-peptidal S-S-bonds.
Amino Acid Sequence↗
Multiple leiomyomata presenting in a child.
We report a 2-year-old boy with a plaque on the upper arm composed of multiple 2- to 3-mm leiomyomata which developed at the age of 3 months and have been unchanged since. Immunohistologically there was positive staining for the muscle intermediate filament desmin. We discuss the unusual clinical presentation and possible prognosis.
Arm↗