Purification and characterization of PK-120, a novel substrate for plasma kallikrein, from guinea pig plasma.
PK-120 is a novel substrate of plasma kallikrein isolated from human plasma. Western blotting using anti-human PK-120 polyclonal antibodies demonstrated the presence of a PK-120-like protein in guinea pig, rat and mouse plasma. We purified the immunoreactive-120 kDa protein from guinea pig plasma by polyethylene glycol fractionation followed by ion-exchange chromatography using Q-Sepharose, heparin-Sepharose, Mono-Q and gel filtration with TSK G3000. The 120 kDa protein thus isolated was similar to human PK-120 with respect to limited proteolysis by kallikrein, amino acid composition, and the N-terminal amino acid sequence, indicating that the immunoreactive 120 kDa protein was guinea pig PK-120.
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Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Nagasawa
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D000595:Amino Acid Sequence; D000818:Animals; D001798:Blood Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D006168:Guinea Pigs; D006493:Heparin; D007610:Kallikreins / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011092:Polyethylene Glycols; D053491:Proteinase Inhibitory Proteins, Secretory; D051381:Rats; D012685:Sepharose
D001798:Blood Proteins; D006023:Glycoproteins; C091236:ITIH4 protein, human; D053491:Proteinase Inhibitory Proteins, Secretory; D011092:Polyethylene Glycols; D006493:Heparin; D012685:Sepharose; D007610:Kallikreins