The serum immunoglobulin concentrations were: IgG 21.6 g/L, IgA 1.2 g/L, IgM 2.64 g/L, κ 7.49 g/L, λ 16.0 g/L, κ/λ 0.47. The results of immunohistochemistry showed cytoplasmic expression of IgE immunoglobulin and λ light chain in the tumor tissue.
The phosphorylation and dephosphorylation of 20KD myosin light chains(MLC20) by Ca2±/ Calmodulin(CaM) dependent myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) play the key role for the regulation in smooth muscle contraction.
2. Identification of McAbs: the immunoglobulin subclasses of A_12B_4C_9C_2, G_4A_3 and G_7A_9 were IgM, IgG2a, IgG1, and IgG1 respectively and the light chains of which were all categorized into chain κ.
The definitive fast muscle contained three light chain types, MLC1, MLC2, and MLC3; slow muscle, MLC1 and MLC3; while the larval muscle fibers included a specific larval MLCL in addition to MLC3.
Ontogenetic and Phylogenetic Analysis of Myosin Light Chain Proteins from Skeletal Muscles of Loach Misgurnus fossilis
mRNAs of all three types of myosin light chain proteins are expressed in skeletal muscles of both larval and adult stages of loach Misgurnus fossilis (Cobitidae) and these proteins are encoded by different genes (mlc1, mlc2, and mlc3).
Our approach (RT-PCR with fish-specific mlc1, mlc2, and mlc3 primers) failed to reveal the larval form of myosin light chain protein found previously by protein electrophoresis of loach fry muscle extract.
Origin and structure of myosin light chain (MLC) proteins have been studied by comparative analysis of fish mlc1, mlc2, and mlc3 genes encoding MLC1, MLC2, and MLC3, respectively.
Development of Quantitative Enzyme Immunoassay and Radioimmunoassay of λ-Free Light Chains of Immunoglobulins
Immunization of BALB/c mice by horse antiserum against diphtheria made it possible to obtain IgG1 monoclonal antibodies (MoAbs) 2B7E4 specific for light chains of horse immunoglobulin (Ig).
Synthesis of the main contractile proteins, primarily the components of myosin molecule-heavy chain (MHC) and individual isoforms of light chains (MLC1, MLC2, and MLC3)-are encoded by different genes during different ontogenetic stages.
Comparative structural analysis of myosin light chains and gene duplication in fish
Phosphorylation of myosin light chains as a result of activation of myosin light chain kinase and inactivation of myosin phosphatases stimulates stress fiber formation and triggers actomyosin contraction.
In their most active forms the toxins exist as dichain molecules in which a heavy (H) chain is linked by disulphide bonding to a light (L) chain.
The VIP binding activity of the soluble and phage-displayed form of this L chain was confirmed by radioimmunoassay and ELISA, respectively.
The light (L) chain of a model antibody (Ab) was deduced to contain a serine protease-like catalytic site capable of cleaving peptide bonds.
The catalytic activity can potentially be improved by somatic sequence diversification and pairing of the L chain with the appropriate heavy chain.
An ATP-binding activity of fractions of sIgA was demonstrated by affinity chromatog raphy on ATP-Sepharose and by covalent binding of an affinity analog of ATP; this activity was mediated by the L chain of sIgA.