Methionyl Soluble Ribonucleic Acid Transforrnylase

نویسندگان

  • HERBERT W. DICKERMAN
  • EDWARD
چکیده

The MO-formyltetrahydrofolate:methionyl soluble ribonucleic acid transformylase has been purified over 1500-fold from Escherichia coli B. Although not homogeneous at this stage, the enzyme was of sufficient purity to determine some physical characteristics. The sedimentation constant was 2.02 which would indicate a molecular weight of approximately 25,000. In addition to the substrates of the reaction a partial dependency on magnesium ion was observed. The identity of the formyl donor was elucidated and found to be No-formyltetrahydrofolate.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The Enzymic Synthesis of Amino Acyl Derivatives of Ribonucleic Acid I. THE MECHANISM OF LEUCYL-, VALYL-, ISOLEUCYL-, AND METHIONYL RIBONUCLEIC ACID FORMATION”

The enzymic formation of enzyme-bound amino acyl adenylates from adenosine triphosphate and amino acid (Equation 1) has been recognized for several years (l-8) and enzymes specific for certain of the amino acids have been isolated in a number of laboratories (2, 9, 10). These same enzymes are now known (11-15) to catalyze a second reaction involving the transfer of the amino acyl moiety from th...

متن کامل

Isolation of 30S and 50S active ribosomal subunits of Bacillus subtilis, Marburg strain.

Active 30S and 50S ribosomal subunits were isolated from Bacillus subtilis. These subunits were able to perform not only protein synthesis in the presence of artificial or natural messenger ribonucleic acid but also the specific functions characteristic of each of the subunits. Thus the 30S subunits alone are able to bind formyl-methionyl-transfer ribonucleic acid, and the 50S subunits carry th...

متن کامل

The aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.

The mechanism of the recognition of methionine by Escherichia coli methionyl-tRNA synthetase was examined by a kinetic study of the recognition of methionine analogues in the ATP-PPi exchange reaction and the tRNA-aminoacylation reaction. The results show that the recognition mechanism consists of three parts: (1) the recognition of the size, shape and chemical nature of the amino acid side cha...

متن کامل

Initiation of protein synthesis by folate-sufficient and folate-deficient Streptococcus faecalis R: partial purification and properties of methionyl-transfer ribonucleic acid synthetase and methionyl-transfer ribonucleic acid formyltransferase.

The initiation of protein synthesis by Streptococcus faecalis R grown in folate-free culture occurs without N-formylation or N-acylation of methionyl-tRNA(f) (Met). Methionyl-tRNA synthetase and methionyl-tRNA formyltransferase were partially purified from S. faecalis grown under normal culture conditions in the presence of folate (plus-folate); the general properties of the enzymes were determ...

متن کامل

The interaction of 'soluble' ribonucleic acid, magnesium ions and sulphydryl groups in the control of amino acid-dependent pyrophosphate-exchange reactions.

During an attempt to purify a leucine-activating enzyme from pig-liver-protein fractions low in 'soluble' ribonucleic acid (Hele & Finch, 1960), some fractions became very unstable and lost over half their activity when kept overnight at 15°. In some instances, enzyme activity has been found to be preserved by the presence of 'soluble' ribonucleic acid. In this paper the effect has been further...

متن کامل

ذخیره 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 نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2003