caa a22 4500 397557175 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021381 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021381 Complete Sequence, Subunit Structure, and Complexes with Pancreatic α-Amylase of an α-Amylase Inhibitor from Phaseolus vulgaris White Kidney Beans [Elektronische Daten] [Keiji Kasahara, Kaeko Hayashi, Tsutomu Arakawa, John S. Philo, Jie Wen, Saburo Hara, Haruki Yamaguchi] The complete amino acid sequence of a white kidney bean (Phaseolus vulgaris) α-amylase inhibitor (PHA-I), which is composed of two kinds of glycopolypeptide subunits, α and β, was established by conventional methods. The polypeptide molecular weight of PHA-I determined by the light-scattering technique, considered together with the sequence molecular weights revealed for the subunits, Indicated that PHA-I has the subunit stoichiometry of (α,β)2 complex. Inhibition test of PHA-I with increasing amounts of porcine pancreatic α-amylase (PPA) suggested that an inactive 2:1 complex is formed between PPA and PHA-I. In fact, two complexes differing from each other in the molar ratio of PPA to PHA-I were separated by gel filtration, and molecular weight estimation by the light-scattering technique confirmed that they are complexes of PHA-I with one or two PPA molecules. The binding of PPA to PHA-I appeared to follow simple binomial statistics, suggesting that two binding sites on PHA-I are independent and of high affinity for PPA. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence α-amylase inhibitor nationallicence complete structure nationallicence inhibition stoichiometry nationallicence kidney bean nationallicence subunit structure nationallicence Kasahara Keiji Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University Gakuen-cho 1-1, Sakai, Osaka 593 aut Hayashi Kaeko Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki Sakyo-ku, Kyoto 606 aut Arakawa Tsutomu Amgen Inc., Thousand Oaks California 91320-1789, USA aut Philo John S. Amgen Inc., Thousand Oaks California 91320-1789, USA aut Wen Jie Amgen Inc., Thousand Oaks California 91320-1789, USA aut Hara Saburo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki Sakyo-ku, Kyoto 606 aut Yamaguchi Haruki Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University Gakuen-cho 1-1, Sakai, Osaka 593 aut The Journal of Biochemistry Oxford University Press 120/1(1996-07), 177-183 0021-924X 120:1<177 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021381 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021381 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kasahara Keiji Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University Gakuen-cho 1-1, Sakai, Osaka 593 aut NATIONALLICENCE 700 1- Hayashi Kaeko Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Arakawa Tsutomu Amgen Inc., Thousand Oaks California 91320-1789, USA aut NATIONALLICENCE 700 1- Philo John S. Amgen Inc., Thousand Oaks California 91320-1789, USA aut NATIONALLICENCE 700 1- Wen Jie Amgen Inc., Thousand Oaks California 91320-1789, USA aut NATIONALLICENCE 700 1- Hara Saburo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Yamaguchi Haruki Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University Gakuen-cho 1-1, Sakai, Osaka 593 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 177-183 0021-924X 120:1<177 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford