The chromatography of the meromyosins on diethylaminoethylcellulose.
نویسندگان
چکیده
In a previous chromatographic study of rabbit L-myosin (Perry, 1960) the distribution of adenosine-triphosphatase activity in the main eluted fraction of this protein did not appear to be compatible with enzymic homogeneity. Brahms (1959, 1960) has also reported the separation of components of different adenosine-triphosphatase activity from rabbit myosin. The relation of these findings to the subunit structure of myosin is far from clear but they suggested that re-investigation of the distribution of adenosine-triphosphatase activity between the light and heavy meromyosins (Szent-Gyorgyi, 1953; Gergely, 1953; Mihalyi & Szent-Gyorgyi, 1953) might throw some light on this problem. There is accumulating evidence of the heterogeneity of the meromyosins (Lowey & Holtzer, 1959; Fryar & Gibbs, 1960; Szent-Gyorgyi, Cohen & Philpott, 1960) and the solubility properties of heavy meromyosin compared to myosin and to light meromyosin make this protein particularly suitable for chromatographic studies with diethylaminoethylcellulose. The present paper is concerned with a chromatographic investigation of the standard light and heavy meromyosin preparations and the distribution of adenosine-triphosphatase activity in the fractions which can be isolated from these proteins. Evidence is presented which suggests that fragments, other than heavy meromyosin, which result from tryptic digestion of myosin, possess appreciable adenosine-triphosphatase activity. A preliminary note of some of the findings reported here has appeared earlier (Mueller & Perry, 1960).
منابع مشابه
Ribonucleotides of RNA: separation by chromatography on sheets of diethylaminoethylcellulose.
The four main ribonucleotides of RNA can be separated on diethylaminoethylcellulose paper sheets, with results comparable to column chromatography, by irrigation with 0.05M formic acid for 2 to 3 hours, and then reversing the direction of irrigation with 4M formic acid.
متن کاملThe chromatography of growth hormone on cellulose derivatives.
In this paper a report is made of the chromatographic behavior of growth hormone on columns of carboxymethylcellulose and diethylaminoethylcellulose. Ion exchange chromatography on the synthetic resin, Amberlite IRC-50, has been utilized to purify and to assess the homogeneity of a number of proteins. This resin has been used in chromatographic studies on cytochrome c (l), ribonuclease (2), lys...
متن کاملCrystallization and properties of aldolase from a transplantable rat sarcoma.
Aldolase was isolated in a crystalline form in a 6% yield from rat Rhodamine sarcomas. The purification involved extraction with Tris-buffer, batchwise treatment with diethylaminoethylcellulose, ammonium sulfate fractionation, column chromatography on cellulose phosphate, and crystallization from ammonium sulfate solution (0.35 saturation). The crystalline aldolase preparation behaved as a homo...
متن کاملCrystallization and Properties of Aldolase from a Transplan table Rat Sarcoma1
Aldolase was isolated in a crystalline form in a 6% yield from rat Rhodamine sarcomas. The purification involved extraction with Tris-buffer, batchwise treatment with diethylaminoethylcellulose, ammonium sulfate fractionation, column chromatography on cellulose phosphate, and crystallization from ammonium sulfate solution (0.35 saturation). The crystalline aldolase preparation behaved as a homo...
متن کاملInduced formation of leucine decarboxylase in Proteus vulgaris.
1. The serum myeloma protein and urinary Bence-Jones protein of mice carrying the MPC-2 plasma-cell neoplasm have been purified by chromatography on ion-exchange diethylaminoethylcellulose and characterized. 2. The neoplastic plasma cells were found to form both proteins. Biosynthesis was studied by incubating sliced tumour tissue in vitro and following the incorporation of [14C]amino acids int...
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 Biochemical journal
دوره 80 شماره
صفحات -
تاریخ انتشار 1961