Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.
1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.
Ohkubo
I
I
Department of Biochemistry, Nagoya City University Medical School, Japan.
Namikawa
C
C
Higashiyama
S
S
Sasaki
M
M
Minowa
O
O
Mizuno
Y
Y
Shiokawa
H
H
D000596:Amino Acids / Q000032:analysis; D001798:Blood Proteins / Q000302:isolation & purification*; D002241:Carbohydrates / Q000032:analysis; D006023:Glycoproteins / Q000097:blood / Q000302:isolation & purification; D006801:Humans; D007704:Kininogens / Q000032:analysis*; D007705:Kinins / Q000032:analysis*; D008970:Molecular Weight; D011480:Protease Inhibitors
D000596:Amino Acids; D001798:Blood Proteins; D002241:Carbohydrates; D006023:Glycoproteins; D007704:Kininogens; D007705:Kinins; D011480:Protease Inhibitors; C034138:alpha-thiol proteinase inhibitor