Amino acid composition of horse heart cytochrome c.

نویسندگان

  • E MARGOLIASH
  • J R KIMMEL
  • R L HILL
  • W R SCHMIDT
چکیده

As the first step in the study of the amino acid sequence of horse heart cytochrome c, it was essential to establish the exact composition of the protein. Although the molecular weight is low (approximately 12,000) (1) and the protein contains less than 110 amino acid residues per mole, analyses by three diierent laboratories (2-4) have not yielded strictly concordant results. These analyses are in agreement to within 1 residue per mole for the content of arginine, proline, methionine, isoleucine, tyrosine, and phenylalanine but vary by 1 residue or more for all of the other amino acids. The relatively recent development of highly accurate automatic recording equipment for the analysis of amino acid mixtures (5) and of an enzymic method for the complete hydrolysis of proteins (6) that obviates some of the difficulties encountered with acid hydrolysis procedures has made it possible to determine precisely the composition and the amide distribution of horse heart cytochrome c.

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

Amino acid sequence of chymotryptic peptides from horse heart cytochrome c.

The preparation, purification, and amino acid composition of peptides obtained from a chymotryptic digest of horse heart cytochrome c have been described in the preceding paper (1). The present work is concerned with the determination of the amino acid sequence of these peptides, which account for the complete composition of the protein. Combining the results of the present work with those of K...

متن کامل

Structural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c

Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...

متن کامل

Isolation and amino acid composition of chymotryptic peptides from horse heart cytochrome c.

Mammalian cytochrome c is a protein of low molecular weight (approximately 12,500) (l-3) containing one heme per mole of protein. Through the efforts of many investigators, our knowledge of its biological function and over-all physicochemical properties is well documented (see reviews by Paul (4), Keilin and Slater (5), and George and Lyster (6)) ; however, there is relatively little informatio...

متن کامل

Amino Acid Sequence of Chicken Heart Cytochrome c

The complete amino acid sequence of chicken heart cytochrome c has been established. This primary structure is typically that of a “mammalian-type” cytochrome c showing the characteristic groupings of hydrophobic and basic residues, and, like the other cytochromes c from vertebrate species, has an acetylated amino-terminal residue. Chicken heart cytochrome c differs from the horse, beef, human,...

متن کامل

The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.

1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from ...

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 237  شماره 

صفحات  -

تاریخ انتشار 1962