69-kDa and 100-kDa Isoforms of Interferon-Induced (2'-5')Oligoadenylate Synthetase Exhibit Differential Catalytic Parameters

Characterization of 69- and 100-kDa forms of 2-5A-synthetase from interferon-treated human cells.

The existence of distinct 69- and 100-kDa forms of 2-5A-synthetase in addition to the smaller (40 and 46 kDa) forms has recently been established. Using specific monoclonal antibodies we investigated the induction, synthesis, and activity of 69- and 100-kDa 2',5'-oligoadenylate (2-5A) synthetases in interferon-treated human Daudi cells. Although induction of these synthetases is detectable in c...

Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms.

The classic myelin basic protein (MBP) splice isoforms range in nominal molecular mass from 14 to 21.5 kDa, and arise from the gene in the oligodendrocyte lineage (Golli) in maturing oligodendrocytes. The 18.5-kDa isoform that predominates in adult myelin adheres the cytosolic surfaces of oligodendrocyte membranes together, and forms a two-dimensional molecular sieve restricting protein diffusi...

Differential expression of the 61 kDa and 63 kDa calmodulin-dependent phosphodiesterases in the mouse brain.

Based on their relative abundance and regulation by Ca2+ and by phosphorylation in vitro, it is thought that the Ca2+/calmodulin-dependent phosphodiesterases (CaM-PDEs) are important modulators of cyclic nucleotide function in the brain. Two of the most abundant CaM-PDEs in the brain are the 61 kDa and 63 kDa isozymes. In this study, the regional and cellular expression of mRNA encoding these t...

Molecular Weight Hymenoptera Venom Characterization of the 100 kDa High

MMP 2 ( matrix metallopeptidase 2 ( gelatinase A , 72 kDa gelatinase , 72 kDa type IV collagenase ) .

Description MMP2 is a Zn dependent endopeptidase, synthesized and secreted in zymogen form. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide'pro' domain that maintains enzyme-latency until cleaved or disrupted, and a catalytic domain that contains the conserved zin...