The amino acid sequence of the pike (<i>Esox lucius</i>) parvalbumin III

Frankenne, Françis; Joassin, L.; Gerday, Ch.

doi:10.1016/0014-5793(73)80597-6

Cited by 39 publications

(12 citation statements)

References 14 publications

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“…With respect to its sequence, the major parvalbumin from thornback ray would appear to belong to both the CI and the p lineages detected previously for muscular parvalbumins [l]. Indeed, the extended, basic, N-terminal region of the ray sequence is reminiscent of that of the three members of the CI lineage known at present: the coelacanth pl-5.4-5.0 component [l], the pike pl-5.0 component [7] and the rabbit pl-5.5 component [12]. On the other hand, the phenylalanine residue of the hydrophobic doublet in position 65/66 is located in position 66 in the ray, a distinct feature of all known members of the lineage such as the hake pl-4.36 component [5], the carp pl-4.25 and pl-4.47 components [6,8], the pike pl-4.…”

Section: Discussionmentioning

confidence: 85%

The Amino-Acid Sequence of the Major Parvalbumin from Thornback-Ray Muscle

Thatcher

Péchère

1977

Eur J Biochem

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ParvalbuminRecherche Scientifique, Montpellier (PI = 4.45) from the cartilagenous fish Raja The primary structure of the major parvalbumin clavata has been determined. The amino acid sequence was dehuced by the analysis of peptides derived from tryptic digestion of the oxidized protein. These peptides were aligned by comparison with (a) overlapping peptides produced by limited tryptic and chymotryptic digestion, and (b) by comparison with the known structures of other fish parvalbumins. The molecular evolution of thornback ray parvalbumin is briefly discussed.The investigation of the molecular evolution of muscular parvalbumins [l] is interesting both in itself and because the close relationship existing between this family of proteins and other proteins, in particular troponin-C and the light chains of myosin. Genetic duplication and genetic fusion seem to have played a remarkable role in the diversification of all these proteins from a single ancestral gene [2-41.Previous work on the primary structure of muscular parvalbumins has been concerned with components isolated from different species of teleostean fishes, [l, 5 -103, from an amphibian [l 1 ] and from a mammal [12,13]. This exploration of the molecular evolution of vertebrate parvalbumins has now been extended by examining the amino acid sequence of the protein from a species considered morphologically primitive. Thornback ray, a cartilagenous fish, was chosen, as previous studies [14,15] had shown that a major parvalbumin could be readily isolated from the muscles of this animal. The present report will describe the establishment of its primary structure as well as those characteristics which show it to be closely related to the molecular ancestor of all presently known parvalbumins. MATERIALS AND METHODS Preparation of the ProteinThornback rays (Raja clavata) were kindly provided by the Institut des Ptches Maritimes, Sete. The Pro teinase Digest ionThe parvalbumin (50 mg) was first oxidized by the method of Hirs [18], desalted into 5 % formic acid and freeze-dried. A solution of 20 mg of oxidized parvalbumin per ml was then made up in 0.05 M ammonium acetate buffer, pH 8.5, 6 M with respect to guanidinium chloride. The protein solution was heated at 50 "C for 4 h, before desalting into 0.05 M ammonium acetate, pH 8.5 on Sephadex G-25. The parvalbumin fractions were pooled and then boiled for 15 min. A thick white precipitate formed on cooling. Trypsin or chymotrypsin were added to the parvalbumin suspension to give a final concentration (w,/w) of 1 : 40 for the proteinase: substrate ratio. The precipitate cleared within 5 min and digestion was allowed to continue for a further hour at 37 "C. The digest was then freeze-dried. Pep tide Fructionut ionBoth the ion-exchange methods developed by Jones [19] and paper methods [20] were used to isolate peptides. Initially tryptic peptides were separated by cation-exchange chromatography, using either a Chromobeads P column or a column of DAI-X2 resin as described previously [ 121. Peptide fractions

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Section: Discussionmentioning

confidence: 85%

The Amino-Acid Sequence of the Major Parvalbumin from Thornback-Ray Muscle

Thatcher

Péchère

1977

Eur J Biochem

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“…As observed for most other parvalbumins (10,12,13), the amino terminus of the rabbit protein is blocked. The entire sequence was, therefore, derived by analysis of peptides produced by specific cleavages of the polypeptide chain.…”

Section: Resultsmentioning

confidence: 54%

“…(10), hake (12), and pike III (13) parvalbumins. The sequence of the rabbit parvalbumin is given in capital letters; of the other parvalbumins, only residues that differ from those of the rabbit are shown.…”

Section: Resultsmentioning

confidence: 99%

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Amino-acid sequence of parvalbumin from rabbit skeletal muscle.

Enfield¹,

Ericsson²,

Blum³

et al. 1975

Proc. Natl. Acad. Sci. U.S.A.

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Determination of the complete aminoacid sequence of rabbit skeletal muscle parvalbumin is described. The sequence of 86 of the 109 total residues was determined automatically by sequenator analyses of peptides obtained after cleavage with CNBr or with trypsin. The positions of the remaining 23 residues were determined by subtractive Edman degradation of tryptic and chymotryptic peptides. The protein has an acetylated amino terminus. Comparison of the rabbit parvalbumin with those from carp, hake, and pike and with the calcium-binding subunit of rabbit muscle troponin indicates that these proteins are homologous. Among the parvalbumins a high degree of identity is observed, especially of residues involved in the binding of calcium or in the formation of the hydrophobic core.

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“…The other case is that of the 5.0 pike component studied by Frankenne et al [24] (and C. Gerday, personal communication), which although encompas- sing only 108 amino acids, clearly suffered a deletion between its second and third residues so that its actual length also corresponds to 109 residues. The pike 5.0 parvalbumin, in addition, has three lysyl doublets at exactly the same positions as in the rabbit parvalbumin, but lacks the remarkable lysyl triplet of the last, only the first of these three lysyl residues being present in the isologous position of the pike parvalbumin.…”

Section: Discussionmentioning

confidence: 97%

Parvalbumin from Rabbit Muscle. Isolation and Primary Structure

Capony¹,

Pina²,

Péchère³

1976

Eur J Biochem

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A parvalbumin, with its characteristic low molecular weight (∼ 12000), acidic isoelectric point (∼ 5.5), ultraviolet spectrum (maxm 259 nm) and Ca2+‐binding capacity (2 mol/mol protein) has been isolated from rabbit (Oryctolagus cuniculus) muscle. Its primary structure has been determined from a study of its tryptic peptides and of overlapping peptides generated by limited tryptic digestion and by chymotryptic and thermolytic digestions of the protein. The amino acid sequence so obtained is considered in comparison with those known for other parvalbumins and for rabbit troponin C.

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The amino acid sequence of the pike (Esox lucius) parvalbumin III

Cited by 39 publications

References 14 publications

The Amino-Acid Sequence of the Major Parvalbumin from Thornback-Ray Muscle

The Amino-Acid Sequence of the Major Parvalbumin from Thornback-Ray Muscle

Amino-acid sequence of parvalbumin from rabbit skeletal muscle.

Parvalbumin from Rabbit Muscle. Isolation and Primary Structure

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