Mechanism of formation of iron(ii) complexes with pentadentate ligands via C–C bond formation between trans-[Fe(2,4-bis(2-pyridylmethylimino)pentane)(MeCN)2][ClO4]2·MeCN and various nitriles

2005 ◽  
pp. 1086-1092 ◽  
Author(s):  
Hiromasa Kurosaki ◽  
Yoshinobu Ishikawa ◽  
Takao Ishihara ◽  
Teruo Yamamoto ◽  
Yoshihiro Yamaguchi ◽  
...  
Antibodies ◽  
2020 ◽  
Vol 9 (4) ◽  
pp. 66
Author(s):  
Carl Mieczkowski ◽  
Soheila Bahmanjah ◽  
Yao Yu ◽  
Jeanne Baker ◽  
Gopalan Raghunathan ◽  
...  

We report the novel crystal structure and characterization of symmetrical, homodimeric humanized heavy-chain-only antibodies or dimers (HC2s). HC2s were found to be significantly coexpressed and secreted along with mAbs from transient CHO HC/LC cotransfection, resulting in an unacceptable mAb developability attribute. Expression of full-length HC2s in the absence of LC followed by purification resulted in HC2s with high purity and thermal stability similar to conventional mAbs. The VH and CH1 portion of the heavy chain (or Fd) was also efficiently expressed and yielded a stable, covalent, and reducible dimer (Fd2). Mutagenesis of all heavy chain cysteines involved in disulfide bond formation revealed that Fd2 intermolecular disulfide formation was similar to Fabs and elucidated requirements for Fd2 folding and expression. For one HC2, we solved the crystal structure of the Fd2 domain to 2.9 Å, revealing a highly symmetrical homodimer that is structurally similar to Fabs and is mediated by conserved (CH1) and variable (VH) contacts with all CDRs positioned outward for target binding. Interfacial dimer contacts revealed by the crystal structure were mutated for two HC2s and were found to dramatically affect HC2 formation while maintaining mAb bioactivity, offering a potential means to modulate novel HC2 formation through engineering. These findings indicate that human heavy-chain dimers can be secreted efficiently in the absence of light chains, may show good physicochemical properties and stability, are structurally similar to Fabs, offer insights into their mechanism of formation, and may be amenable as a novel therapeutic modality.


1976 ◽  
Vol 160 (3) ◽  
pp. 745-755 ◽  
Author(s):  
S Hayakawa ◽  
S Hashimoto ◽  
T Onaka

The metabolism of cholic acid (I) by Streptomyces rubescens was investigated. This organism effected ring A cleavage, side-chain shortening and amide bond formation and gave the following metabolites: (4R)-4-[4α-(2-carboxyethyl)-3aα-hexahydro-7aβ-methyl-5-oxoindan-1 β-yl]valeric acid (IIa) and its mono-amide (valeramide) (IIb); and 2,3,4,6, 6aβ,7,8,9,9aα,9bβ-decahydro-6aβ-methyl-1H-cyclopenta[f]quinoline-3,7-dione(IIIe)and its homologues with the β-oriented side chains, valeric acid, valeramide, butanone and propionic acid, in the place of the oxo group at C-7, i.e.compounds (IIIa), (IIIb), (IIIc) and (IIId) respectively. All the nitrogenous metabolites were new compounds, and their structures were established by partial synthesis except for the metabolite (IIIc). The mechanism of formation of these metabolites is considered. A degradative pathway of cholic acid (I) into the metabolites is also tentatively proposed.


Author(s):  
A. A. Safronov ◽  
V. S. Dub ◽  
V. V. Orlov ◽  
K. L. Kosyrev ◽  
A. S. Loskutov ◽  
...  

Author(s):  
I.V. Mitin ◽  
◽  
I.R. Tatur ◽  
K.U. Smirnov ◽  
A.M. Suloev ◽  
...  

The reasons for the formation of varnish deposits of turbine oils are determined. It is shown that the performance of turbine oils is determined by methods of ASTM D7843 (MPC) and ASTM D6971 (RUL) can be assessed, the process of formation of varnish deposits, the level of antioxidant properties, antioxidant content of, amend, and extend the oil change, and to predict critical situation in the operation of turbine equipment. The mechanism of formation of varnish deposits in turbine oils is proposed.


Sign in / Sign up

Export Citation Format

Share Document