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Biomedical subjects

G Chiericato

Publications and source records attributed to G Chiericato.

4 recordsLinked to original sources
PubMed2001

4-Cyanopyridine and amide-N and amide-O linkage isomers of 4-pyridinecarboxamide on trans-chloro(1,4,8,11-tetraazacyclotetradecane)ruthenium(II/III).

The synthesis, UV-vis spectra, and electrochemical behavior of the nitrile-bonded trans-[Ru(II)Cl(cyclam)(4-NCpyH(+))](BF(4))(2) (4-Ncpy = 4-cyanopyridine; cyclam = 1,4,8,11-tetraazacyclotetradecane) and of trans-[Ru(III)Cl(cyclam)(NHC(O)-4-pyH(+))](2+) are described. The UV-vis spectrum of the Ru(II) nitrile complex shows a MLCT band at 548 nm at pH 1, which is shifted to 440 nm at pH approximately 6, for the unprotonated species. trans-[Ru(II)Cl(cyclam)(4-NCpyH(+))](2+) was electrolytically oxidized (+600 mV vs Ag/AgCl) at pH 1 to Ru(III), followed by hydrolysis (k = 0.25 s(-1)) of the coordinated nitrile to give trans-[Ru(III)Cl(cyclam)(NHC(O)-4-pyH(+))](2+), in which the amide is deprotonated and coordinated through nitrogen. The identity of the species is pH dependent, the nitrogen-bonded amide prevailing at low pH (< 7), but the oxygen-bonded amide is formed through linkage isomerization at higher pH (>8). Reduction of trans-[Ru(III)Cl(cyclam)(NHC(O)-4-pyH)](2+) in acidic media does not result in fast aquation (k = approximately 2.4 x 10(-5) s(-1)) as for other amides on ruthenium(II) pentaammine, but instead linkage isomerization occurs, resulting in the oxygen-bonded species, with an estimated rate constant of approximately 2 x 10(-2) s(-1), smaller than in the pentaammine analogues.

Journal Article↗
PubMed1976

Sheep prothrombin: purification and partial characterization.

A procedure for the preparation of highly purified sheep prothrombin is described. The purified zymogen, when subjected to disc gel electrophoresis in polyacrylamide, gave rise to one single band. Only alanine was found as N-terminal residue. Carboxypeptidases A and B failed to release any C-terminal residue. The isoelectric point, as determined by isoelectric focusing in polyacrylamide gel slab, was shown to be 4.9-5.0. Non-chromatographed, but not the purified zymogen, could be converted into active thrombin in half-saturated trisodium citrate seeded with thrombin. Pure sheep prothrombin showed 5.6% of neutral sugars and the following amino acid composition: Ala35, Arg44, Asx54-55, -Cys24, Glx72, Gly53-54, His8, Ile19, Leu45, Lys31, Met7, Phe23, Pro36, Ser34, Thr29-29, Trp16, Tyr19 and Val33, which accounts for a molecular weight of about 66 000 (amino acids only). The molecular weight as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis after reduction by 2-mercaptoethanol, was shown to be 77 000 +/- 3000 (carbohydrates included).

Amino Acids↗
PubMed1976

Amino acid sequence of penicillopepsin. IV. Myxobacter AL-1 protease II and Staphylococcus aureus protease fragments and homology with pig pepsin and chymosin.

The digest of penicillopepsin (EC 3.4.23.7) with protease II from Myxobacter AL-1 gave five fragments which were separated on a Biogel P-100 column in 70% formic acid. The fragments were from 16 to 125 amino acids long. Two fragments were also isolated from a digest with a protease from Staphylococcus aureus. The analysis of these fragments by automatic sequencer gave a number of overlaps of the chymotryptic and thermolytic peptides. The available amino acid sequence data for penicillopepsin described in this paper and the accompanying papers (Kurosky, A. and Hofmann, T.:Can. J. Biochem. 54, 872 (1976);Rao, L and Hofmann, T.:Can. J. Biochem.54,885 (1976); Harris, C.I.,Rao, L., Shutsa, P., Kurosky, A. and Hofmann, T.: Can. J. Biochem. 54,895 (1976) have been combined and yield 15 fragments which range in lengths from 3 to 112 amino acid residues. These unique fragments account for virtually all the amino acids of the fungal protease. Four of the fragments with a total of 194 residues (about 60% of the molecule) have been aligned with corresponding sections of pig pepsin (EC 3.4.23.1) and with part of the N-terminal sequence available for calf chymosin (EC 3.4.23.4). In the alignments about 37% of the residues in the fungal enzyme are identical with at least one of the mammalian enzymes. An additional 20% are chemically similar. These results, together with previously reported active site directed modifications, show conclusively that penicillopepsin is an evolutionary homologue of the mammalian acid proteases.

Amino Acid Sequence↗