Charge control in the formation of complexes of phenol with ethylene derivatives containing organoelemental group IVB substituants

A. N. Egorochkin; S. E. Skobeleva; V. L. Tsvetkova

doi:10.1007/bf00699922

Charge control in the formation of complexes of phenol with unsaturated compounds containing organometallic substituents from group IV

Russian Chemical Bulletin ◽

10.1007/bf01558061 ◽

1994 ◽

Vol 43 (6) ◽

pp. 976-982

Author(s):

A. N. Egorochkin ◽

S. E. Skobeleva ◽

E. T. Bogoradovsky ◽

T. P. Zubova

Keyword(s):

Group Iv ◽

Charge Control ◽

Unsaturated Compounds ◽

Formation Of Complexes

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NMR and EPR studies on the charge transfer and formation of complexes through incompletely coordinated states

Solid State Ionics ◽

10.1016/s0167-2738(97)00133-1 ◽

1997 ◽

Vol 101-103 (1-2) ◽

pp. 387-392 ◽

Cited By ~ 2

Author(s):

M Senna

Keyword(s):

Charge Transfer ◽

Formation Of Complexes

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Mutations which Introduce Free Cysteine Residues in the Gla-Domain of Vitamin K Dependent Proteins Result in the Formation of Complexes with α1-Microglobulin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650223 ◽

1996 ◽

Vol 75 (01) ◽

pp. 070-075 ◽

Cited By ~ 20

Author(s):

E G C Wojcik ◽

P Simioni ◽

M v d Berg ◽

A Girolami ◽

R M Bertina

Keyword(s):

Vitamin K ◽

Protein C ◽

Cysteine Residue ◽

Factor Ix ◽

Disulphide Bond ◽

Clotting Factors ◽

High Molecular Weight Complex ◽

Low Concentrations ◽

Gla Domain ◽

Formation Of Complexes

SummaryWe have previously described a genetic factor IX variant (Cys18→Arg) for which we demonstrated that it had formed a heterodimer with armicroglobulin through formation of a disulphide bond with the remaining free cysteine residue of the disrupted disulphide bond in the Gla-domain of factor IX. Recently, we observed a similar high molecular weight complex for a genetic protein C variant (Arg-1→Cys). Both the factor IX and the protein C variants have a defect in the calcium induced conformation. In this study we show that the aminoterminus of this protein C variant is prolonged with one amino acid, cysteine. This protein C variant, as well as protein C variants with Arg9→Cys and Ser12→Cys mutations which also carry a free cysteine residue, are shown to be present in plasma as a complex with α1-microglobulin. A prothrombin variant with a Tyr44→Cys mutation, had not formed such a complex. Furthermore, complexes between normal vitamin K-dependent clotting factors and α1-microglobulin were shown to be present in plasma at low concentrations. The data suggest that the presence of an unpaired cysteine residue in the propeptide or the N-terminal half of the Gla-domain has strongly promoted the formation of a complex with α1-microglobulin in the variants.

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Western Blot Analyses of Prekallikrein and its Activation Products in Human Plasma

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648157 ◽

1991 ◽

Vol 65 (04) ◽

pp. 382-388 ◽

Cited By ~ 9

Author(s):

Dulce Veloso ◽

Robert W Colman

Keyword(s):

Complex Formation ◽

Western Blot ◽

Human Plasma ◽

Contact System ◽

Plasma Activation ◽

Normal Plasma ◽

Sds Page ◽

Activation Products ◽

Major Antigen ◽

Formation Of Complexes

SummaryPrekallikrein (PK), a zymogen of the contact system, and its activation products, kallikrein (KAL), KAl-inhibitor complexes and fragments containing KAL epitope(s) have been detected in human plasma by immunoblotting with a monoclonal anti-human plasma PK antibody, MAb 13G1L. Detection of antigen-MAb 13G11 complexes with peroxidase-conjugated anti-IgG showed that the two variants of PK (85- and 88-kDa) are the only major antigen species in normal, non-activated plasma. Upon plasma activation with kaolin, the intensity of the PK bands decreased with formation of complexes of KAL with CL inhibitor (C1 INH) and α2-rrtzcroglobulin (α2M) identical to those formed by the purified proteins. Immunoblots of normal plasma showed good correlation between the PK detected and the amount of plasma assayed. Increasing amounts of KAL incubated with a constant volume of PK-deficient plasma showed increasing amounts of KAL and of KAL-C1 INH and KAL-α2M complexes. Complexes of KALantithrombin III (ATIII) and the ratio of KALα2M/ KAL-CL INH were higher in activated CL INH-deficient plasmas than in activated normal plasmas. Protein resolution by 3-12% gradient SDS-PAGE and epitope detection with [125I]MAb 13G11 showed four KALα2M species and a 45-kDa fragment(s) in both surface-activated normal plasma and complexes formed by purified KAL and α2M. Immunoblots of activated plasma also showed bands at the position of KALCL INH and KALATIII complexes. When α1-antitrypsin Pittsburgh (cα1-AT, Pitts) was added to plasma before activation, KAL-α1-ALPitts was the main complex. The non-activated normal plasma revealed only an overloaded PK band. This is the first report of an antibody that recognizes KAL epitope(s) in KAL-α2M, KALATIII and KALa1-α1Pitts complexes and in the 45-kDa fragment(s). Therefore, MAb 13G11 should be useful for studying the structure of these complexes as well as the mechanism of complex formation. In addition, immunoblotting with MAb 13G11 would allow detection of KAl-inhibitor complexes in patient plasmas as indicators of activation of the contact system.

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