Studies on adenosine triphosphate transphosphorylases. II. Amino acid composition of adenosine triphosphate-creatine transphosphorylase.
نویسندگان
چکیده
Some of the physical and chemical properties of crystalline adenosine triphosphate-creatine transphosphorylase from rabbit muscle (1) have been previously described (2). In 1956, Friedberg reported on the amino acid composition of this enzyme (3). His data, however, were derived from analyses of only two samples hydrolyzed for the same time interval. Preliminary amino acid analyses from this laboratory (4) indicated serious discrepancies from his data and necessitated a more complete study, which is the subject of this paper.
منابع مشابه
Studies on Adenosine Triphosphate Transphosphorylases
The isolation of the crystalline enzymes, adenosine triphosphate-creatine transphosphorylase (1) and adenosine triphosphate-adenosine 5’-phosphate transphosphorylase (2), made possible a comparative approach to the general problem of the mechanism of action of the adenosine triphosphate transphosphorylases. The present series of papers extends earlier studies from this laboratory on these enzym...
متن کاملNucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). 3. Subunit structure of the crystalline enzyme from brewers' yeast.
Previous physical studies from this laboratory by sedimentation velocity and ditfusion and by sedimentation equilibrium (YuE, R. H., RATLIFF, R. L., AND KWY, S. A. (1967) Biochemistry 6, 2923-2932) have permitted an assignment of the kinetic molecular weight of the crystalline brewers’ yeast nucleoside diphosphokinase, namely 102,000 ( 12,000) at infinite dilution. The observed concentration de...
متن کاملKinetic properties and equilibrium constant of the adenosine triphosphate-creatine transphosphorylase-catalyzed reaction.
catalyzed by adenosine triphosphate-creatine transphosphorylase can be described by a reasonable kinetic scheme. It was shown that MgATPzis the “true substrate,” that the Michaelis constant is the dissociation constant of the enzyme-substrate complex, and that the pH-activity curve resembles a single ionization curve with pK N 6.5. It was of interest to study the kinetics of the reverse process...
متن کاملIsolation of the human ATP-creatine transphosphorylases (creatine phosphokinases) from tissues of patients with Duchenne muscular dystrophy.
Detailed procedures are described for the separation and isolation of the isoenzymes of ATP-creatine transphosphorylase (creatine phosphokinase) from autopsy samples of muscle and brain tissue of five terminal dystrophic males (x-linked, Duchenne). These direct isolation studies have led to the remarkable observation that three isoenzymes are present in the atrophied muscle tissue (characterize...
متن کاملThe Effect of Vitrification and in vitro Culture on the Adenosine Triphosphate Content and Mitochondrial Distribution of Mouse Pre-Implantation Embryos
Background: The mitochondria are an important source of adenosine triphosphate (ATP) production in pre-implantation embryo. Therefore, the objective of this study was to investigate the effect of vitrification and in vitro culture of mouse embryos on their mitochondrial distribution and ATP content. Methods: The embryos at 2-PN, 4-cell and blastocyst stages were collected from the oviduct of st...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 237 شماره
صفحات -
تاریخ انتشار 1962