The estimation of threonine and serine in proteins

Rees, M. W.

doi:10.1042/bj0400632

Cited by 278 publications

(54 citation statements)

References 11 publications

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“…Threonine and serine values were corrected for hydrolytic loss (30 given for those regions with a coding capacity of MW > 10,000 (6). The positions of potential promoters conforming to the core (6) consensus sequence TATA and polyadenylation signals AATAA are also shown.…”

Section: Northern Hybridizationsmentioning

confidence: 99%

Bidirectional transcription of maize streak virus DNA and identification of the coat protein gene

et al. 1985

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Three RNA transcripts encoded by maize streak virus DNA were detected in polyadenylated RNA from virus-infected maize leaves.Two of the transcripts, a major 0.9kb and a minor 1.05kb RNA, were mapped on the virion (+) sense DNA and the other minor transcript of 1.2kb was mapped on the complementary (-) sense DNA, demonstrating that transcription of MSV DNA was bidirectional.The two virion sense transcripts were 3' coterminal at nucleotide 1114 but had 5' termini at nucleotides 2682 and 163 respectively. Virus-specific polyadenylated RNA translated in vitro to produce a 28,000MW polypeptide, specifically immunoprecipitable by antiserum raised against whole virus. The mRNA for this protein was mapped by hybrid-arrested translation to the long open reading frame in virion sense DNA whose potential amino acid composition, calculated from nucleotide sequence data, closely agreed with that determined experimentally for the coat protein.

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Section: Northern Hybridizationsmentioning

confidence: 99%

Bidirectional transcription of maize streak virus DNA and identification of the coat protein gene

et al. 1985

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“…Appreciable amounts of threonine and serine are also decomposed in the course of acid hydrolysis, with the formation of ammonia. The values for these amino acids and for ammonia have been corrected in accordance with the estimates of Rees for the extent of decomposition (17). His estimates are probably applicable here (14).…”

Section: S O M E Properti~es O F H I S T O N E Smentioning

confidence: 60%

The Amino Acid Composition and Some Properties of Histones

Daly

Mirsky

Ris

1951

Journal of General Physiology

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In this paper the properties and the amino acid compositions of a group of histories and of a protamine-like material are described. Histones have been prepared from a variety of sources, and are now believed to occur in the nuclei of the somatic ceils of most organisms. We have studied the amino acid compositions of histones prepared from calf liver, calf thymus, and fowl erythrocytes. The results have a bearing on the problem of whether histones prepared from different tissues of the same animal or from different animals vary in their amino acid compositions.Protamines have been found in the nuclei of the sperm of many fish, but it is not known whether they occur in other tissues of these fish or in the sperm of other higher animals. We have prepared a protamine-like material from the sperm of the fowl. Its preparation, properties, and amino acid composition are described in detail. The preparation of the fowl erythrocyte histone and the protamine of fowl sperm makes it possible to compare the basic proteins of nuclei in the somatic and sperm cells of the same animal.As histones are among the principal constituents of chromosomes, efforts have been made to determine their role in the structural organization of the chromosome. The action of proteolytic enzymes has sometimes been employed for this purpose (1, 2). The interpretation of such experiments depends on some knowledge of the action of the enzyme employed on the individual components of the chromosome. In order to investigate the validity of the conclusions drawn from such experiments, we have studied the action of pepsin on histones both when isolated and when in the chromosome. Studies of the specificity of proteolyfic enzymes have emphasized the importance of the nature of the amino acids adjacent to the sensitive peptide bond (3). Therefore one of the important factors determining whether a protein will be digested by pepsin is the amino acid composition of the protein. We have found that pepsin does digest histones, and that its action is not surprising in view of the amino acid compositions of the histones.Protamines were first isolated by Miescher from salmon sperm (4). They

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“…T o establish a basis for assessing the results the serine content of gliadin was determined (27) and found to be 4.9% by weight. Gliadin, of molecular weight 30,000, on cleavage of all peptide bonds attached to serine N should therefore yield material containing about 15 fragments with an average chain length of 15-16 residues and with 0.65y0 amino N (3.7% of total N) Can.…”

Section: Resultsmentioning

confidence: 99%

The Action of Sulphuric Acid on Gliadin: With Special Reference to the N-Peptidyl→o-Peptidyl Bond Rearrangement

Ramachandran¹,

McConnell²

1955

Can. J. Chem.

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Treatment of gliadin with sulphuric acid transposes peptide bonds of serine from the amino t o the hydroxyl group. Maximum transposition, 60-70% of the theoretica1, occurs when the protein is treated with anhydrous sulphuric acid a t 0°C. for 35 hr. No rearrangement was detected a t threonine residues. Examination of the peptide materiaI, obtained from the rearranged protein by Elliott's degradation method, indicates apparent "hon~ogeneity". In an alternative scheme for the degradation, nitrous acid deamination of free amino groups was used. The resulting loss in serine content of the protein is direct evidence for the acyl migration of peptide bonds. Incorporation of sulphur and partial disappearance of several amino acids accompany the sulphuric acid treatment. The occurrence of these secondary reactions imposes limitations on the use of sulphuric acid as a reagent for the specific fission of peptide bonds. INTRODUCTIONAttention has recently been directed towards methods which effect fragmentation of protein molecules in a predictable manner. Especially significant is Elliott's procedure for the cleavage of peptide bonds (7, 8, 9) a t the amino groups of the P-hydroxyamino acids, serine and threonine. I t is based on the strong acid-induced N-acyl+O-acyl transformations studied earlier by Bergmann, Brand, and Weinmann (2), Desnuelle and Casal ( 5 ) , and Desnuelle and Bonjour (G), and is briefly outlined in the equations below:. . This N-acyl+O-acyl migration might also occur ~vllere the €-amino groups of f hydroxylysine (26) are linlied in a peptide bond.The treatment of silk fibroin with 97.5% sulphuric acid for three days a t 20°C. (8) caused rearrangelllent in only 66% of the serine residues, the major N-terminal residue detected by the dinitrolluorobenzene method (24) being serine. The non-reactivity of the other serine residues was thought t o result 1AIanuscript received M a y 26, 1955.

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The estimation of threonine and serine in proteins

Cited by 278 publications

References 11 publications

Bidirectional transcription of maize streak virus DNA and identification of the coat protein gene

Bidirectional transcription of maize streak virus DNA and identification of the coat protein gene

The Amino Acid Composition and Some Properties of Histones

The Action of Sulphuric Acid on Gliadin: With Special Reference to the N-Peptidyl→o-Peptidyl Bond Rearrangement

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