髓鞘碱性蛋白肽与IAk之间的短寿命复合物
Short-lived complexes between myelin basic protein peptides and IAk.
作者信息
Mason K, McConnell H M
机构信息
Department of Chemistry, Stanford University, CA 94305.
出版信息
Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12463-6. doi: 10.1073/pnas.91.26.12463.
Abstract
Kinetic rate constants and the equilibrium dissociation constant have been determined for the reaction between an affinity-purified class II major histocompatibility complex molecule IAk and a myelin basic protein analogue peptide, fluorescein-labeled Ac(1-14)A4C15. Under the experimental conditions used, the lifetime of the peptide-free IAk molecule with respect to inactivation is 3.1 hr. The equilibrium dissociation constant, 3.3 +/- 1.7 microM, is determined from measurements of the kinetics of peptide inhibition of IAk inactivation. The measured peptide dissociation halftime is relatively short, 30 min, and the deduced association rate is 100 M-1.s-1. The rate constants and the equilibrium constant are similar to those characteristic of kinetic intermediates in reactions of peptides and class II proteins that lead to long-lived terminal complexes.
摘要
已测定了亲和纯化的II类主要组织相容性复合体分子IAk与髓鞘碱性蛋白类似物肽（荧光素标记的Ac(1-14)A4C15）之间反应的动力学速率常数和平衡解离常数。在所使用的实验条件下，无肽IAk分子失活的半衰期为3.1小时。平衡解离常数为3.3±1.7微摩尔，通过测量肽对IAk失活的抑制动力学来确定。测得的肽解离半衰期相对较短，为30分钟，推导的缔合速率为100 M-1·s-1。这些速率常数和平衡常数与导致长寿命末端复合物的肽和II类蛋白质反应中动力学中间体的特征相似。
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