@article{oai:niigata-u.repo.nii.ac.jp:00016674,
 author = {藤田, 聡},
 issue = {6},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Jun},
 note = {A 138kDa protein, immunoreactive with an antibody to myosin binding subunit　(MBS) of chicken gizzard myosin light chain phosphatase( MLCP), was detected in microsomes as well as myofubrillar fraction from porcine aorta. The 138kDa protein that was purified by immunoprecipitation with the antibody either from microsomes or myofibrillar fraction was found to be a good substrate for cGMP-dependent protein kinase(PKG). The microsomal protein was tightly associated with membranes and could be solubilized by Triton X-100, a property reminiscent of G_1 phosphoprotein, the unidentified major PKG substrate in the vascular smooth muscle. Both proteins co-migrated on SDS-PAGE and the MBS antibody immunoprecipitated thiophosphorylated G_1. Thus, MBS is a substrate for PKG, and the membrane-bound MBS may be identical to G_1, or at least its constituent. We propose that phosphorylation of MBS by PKG may be responsible for cGMP-induced Ca^<2+>-desensitization of contractile machinery in vascular smooth mustle.},
 pages = {334--343},
 title = {血管平滑筋に存在するミオシン軽鎖脱リン酸化酵素のミオシン結合サブユニットについて: cGMP依存性タンパク質リン酸化酵素蔓によるリン酸化とG_1リン酸化タンパク質との類似性},
 volume = {112},
 year = {1998}
}