The subunits of dogfish M4 lactic dehydrogenase.

نویسندگان

  • W S Allison
  • J Admiraal
  • N O Kaplan
چکیده

Treatment of dogfish l& lactic dehydrogenase with carboxypeptidase A releases 1 mole of phenylalanine per 36,000 g of the enzyme and no other amino acids. A mixture of carboxypeptidases A and B releases 1 mole of phenylalanine and 1 mole of lysine per 36,000 g of the lactic dehydrogenase. The amino terminus of dogfish M4 lactic dehydrogenase does not react with either dansyl chloride or the Edman reagent under dissociating conditions. An acylated amino-terminal peptide, acyl-Thr-Ala-Leu, has been specifically isolated from a subtilisin digest of dogfish M4 lactic dehydrogenase. Amino acid analysis of dogfish M4 lactic dehydrogenase indicates that there are 9 arginine residues per 36,000 g of enzyme. Nine unique arginine peptides have been specifically isolated from a tryptic digest of dogfish Mb lactic dehydrogenase in yields approaching 1 mole of peptide per 36,000 g of digest. It has been concluded from these results that dogfish Mq lactic dehydrogenase is composed of four identical polypeptide chains with a molecular weight of 36,000.

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 amino acid sequence of the tryptic peptides isolated from dogfish M4 lactate dehydrogenase.

The peptides which result from treatment of the S-[14C]carboxymethyl derivative of dogfish M4 lactate dehydrogenase (EC 1.1.1.27) with trypsin have been isolated and their sequences have been elucidated. Each identical subunit has a molecular weight of 36,000 and on the basis of the amino acid composition 40 unique tryptic peptides are anticipated. Thirty-seven of these peptides have been isola...

متن کامل

Physical and chemical properties of reversibly inactivated lactate dehydrogenases.

The effect of reversible inactivation on the physical and chemical properties of dogfish M4 and chicken heart H* lactate dehydrogenases has been studied. Reduced diphosphopyridine nucleotide was found to have a significant effect on the rate of recovery of the enzymatic activity, but not on the over-all recovery. Optical rotatory dispersion, circular dichroism, fluorescence, and immunological s...

متن کامل

Synthesis and Degradation of Rat Liver Lactate Dehydrogenase M4 HYBRIDIZATION IN THE PURIFICATION OF LACTATE DEHYDROGENASE

For the measurement of lactate dehydrogenase (LDH) isoenzyme biosynthesis a new method is presented which is based on the quantitative hybridization of isoenzyme MI with isoenzyme Hq. After reversible dissociation the formation of active LDH M4 was more rapid and occurred to a greater extent than the formation of LDH Hq. The formation of hybrid isoenzymes from the two subunits resulted in an in...

متن کامل

Synthesis and degradation of rat liver lactate dehydrogenase M4. Hybridization in the purification of lactate dehydrogenase isoenzymes.

For the measurement of lactate dehydrogenase (LDH) isoenzyme biosynthesis a new method is presented which is based on the quantitative hybridization of isoenzyme MI with isoenzyme Hq. After reversible dissociation the formation of active LDH M4 was more rapid and occurred to a greater extent than the formation of LDH Hq. The formation of hybrid isoenzymes from the two subunits resulted in an in...

متن کامل

Comparative Study on the Conformational Mobility of Muscle Lactate Dehydrogenase from Loach Fish Adapted to Different Temperatures Using Differential Scanning Microcalorimetry

Differential scanning microcalorimetry was used to assess the conformational stability of muscle lactate dehydrogenase (M4-LDH) from skeletal muscle of Misgurnus fossilis (loach) fishes adapted to low (the “cold” enzyme) and high (the “warm” enzyme) environmental temperatures. It was found that the denaturation temperature Td was the same for both forms of lactate dehydrogenase, whereas the den...

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:
  • The Journal of biological chemistry

دوره 244 17  شماره 

صفحات  -

تاریخ انتشار 1969