Interferon-kappa, a novel type I interferon expressed in human keratinocytes.

High throughput cDNA sequencing has led to the identification of interferon-kappa, a novel subclass of type I interferon that displays approximately 30% homology to other family members. Interferon-kappa consists of 207 amino acids, including a 27-amino acid signal peptide and a series of cysteines conserved in type I interferons. The gene encoding interferon-kappa is located on the short arm of chromosome 9 adjacent to the type I interferon gene cluster and is selectively expressed in epidermal keratinocytes.

[Rapid time-resolved fluoroimmunometric analysis of myoglobin].

High performance quantitative procedure for evaluation of myoglobin in blood serum is developed. The principle of two-site immunometry was used involving monoclonal antibodies against nonoverlapping epitopes of myoglobin molecule. The fluorescent compound containing europium served as a label of the antibody.

[Immune electron microscope localization of RNA-polymerase on the Escherichia coli chromosome using monoclonal antibodies against the beta-subunit].

Possibility of the immunoelectron microscopic visualization of RNA polymerase on the Escherichia coli chromosome with monoclonal antibodies against the beta-subunit labelled by [protein A.gold] complex was demonstrated. Using this method RNA polymerase molecules were revealed within nucleoid as well as on the membrane-free chromosome.

[A simple method of determination of antigenic determinants in proteins with known primary structure].

A simple and rapid method is proposed for the localization of antigenic determinants in proteins of known primary structure exemplified by human myoglobin. The polypeptide chain of myoglobin was cleaved with BrCN (at Met residues) or with bromosuccinimide (at Trp and Tyr residues) under conditions which on average gave less than one scission per myoglobin molecule. The "single-hit" cleavage products were separated by gel electrophoresis and transferred to nitrocellulose by electroblotting.