Purification, characterization and developmental expression of pig liver PSP.
We have isolated a perchloric acid-soluble protein designated as PL-PSP from the post-mitochondria supernatant fraction of pig liver. It is soluble in 5% perchloric acid and purified by ammonium sulfate fractionation and CM-Sephadex chromatography. The PL-PSP showed approximately 80-90% homology with PSP isolated from rat liver (RL-PSP) with its partial amino acid sequences. The protein has a molecular mass of approximately 14 kDa which was slightly higher than that of RL-PSP. It inhibited protein synthesis in a rabbit reticulocyte lysate system. The expression of PL-PSP was predominant in liver, kidney and duodenum, and was also expressed in stomach, lung and brain. PL-PSP expression in liver increased from the 1st day to the 1st month. Thus, our findings are the first report on the presence of a PSP in porcine tissues which may be involved in the regulation of cellular growth and differentiation.
Kaneki
K
K
Department of Veterinary Medicine, Faculty of Agriculture, Kagoshima University, 890-0065, Kagoshima, Japan.
Matsumoto
M
M
Suzuki
K
K
Akuzawa
M
M
Oka
T
T
D000367:Age Factors; D000595:Amino Acid Sequence; D000818:Animals; D018507:Gene Expression Regulation, Developmental; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification*; D015151:Immunoblotting; D007150:Immunohistochemistry; D007422:Intestines / Q000737:chemistry; D007668:Kidney / Q000737:chemistry; D008099:Liver / Q000737:chemistry; D012260:Ribonucleases / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification*; D013552:Swine; D014018:Tissue Distribution
D006360:Heat-Shock Proteins; D012260:Ribonucleases