On the Structure of Lysozyme

Ohno, Ko

doi:10.1093/oxfordjournals.jbchem.a126446

Cited by 20 publications

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“…Upon heating proteins with anhydrous hydrazine, all but the C-terminal amino acids were transformed into hydrazides which were separated as the benzal derivatives from the originally C-terminal and now free amino acids 2 Ohno later made use of fluorodinitrobenzene (FDNB) and separation of acidic from neutral dinitrophenyl (DNP) products as a means of separating the free amino acids from the hydrazides. [3][4][5] In the present study a combination of the two procedures has given the best results. The DNP derivatives of the C-terminal amino acids were identified and determined by the twodimensional chromatographic technique of Levy.6•7…”

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confidence: 65%

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Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹

Niu¹,

Fraenkel‐Conrat²

1955

J. Am. Chem. Soc.

199

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confidence: 65%

“…The recovery factors for all amino acids as listed on Table II are the mean values from 4 to 10 experiments in the presence or absence of equimolar protein. The values vary to a certain extent with each experiment.…”

Section: Methodsmentioning

confidence: 99%

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹

Niu¹,

Fraenkel‐Conrat²

1955

J. Am. Chem. Soc.

199

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“…Since analysis of a chemical hydrolyzate of a protein does not distinguish glutamine from glutamic acid, or asparagine from aspartic acid, we have estimated the abundance of these amino acids as follows: the published amide content of each protein was BIOCHEMISTRY: GAMOW AND YCAS assigned to glutamine and asparagine in the ratio in which glutamic and aspartic acid occur in the chemical hydrolyzate. This procedure was unnecessary for insulin, ACTH, lysozyme (20), and zein, where the actual content of the four acids is known. The data on the amide content of tobacco mosaic virus protein are from Schramm (21).…”

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Statistical Correlation of Protein and Ribonucleic Acid Composition

Gamow

Yčas²

1955

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

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Empirical evidence indicates with increasing clearness that ribonucleic acid (RNA) plays a vital role in protein synthesis. It appears rational to assume that the sequence of amino acids characterizing a given protein is uniquely determined by the sequence of nucleotides in the ribonucleic acid molecule.While RNA is a polymer of four different nucleotides, proteins are polymers of 20 different amino acids. Since it is possible to form 20 kinds of triplets from four different elements, this suggests that each of the 20 amino acids is determined by a triplet of nucleotides, taken without regard to order.'The fact that the internucleotide distances are comparable with the distances of amino acid residues in a protein when both are in the extended form makes it plausible that a given amino acid shares its determining nucleotides with neighboring amino acids-. This would necessitate a correlation between neighboring residues in protein sequences, making certain pairs favored and others excluded (1,2). However, studies by Gamow, Rich, and Ycas (2) show that there does not appear to be any such interresidue correlation, and all sequences are apparently possible. Thus it appears more probable that the number of determining nucleotides exceeds by a factor of 3 the number of amino acid residues in the synthesized protein, so that neighboring residues do not share determining nucleotides.It is not possible to test this hypothesis critically against available information on amino acid sequences, since all sequences are permitted. However, the model predicts that the statistical frequency of amino acid residues in proteins will show certain regularities. We have therefore attempted to test whether the distribution of amino acids predicted from the proposed model corresponds with analytically found distributions.If one arranges the amino acids in a protein in order of abundance, repeats this on a collection of proteins,2 and takes the mean values (without regard to identity) of the most abundant, second most abundant, third most abundant, etc., one obtains a curve shown in Figure 1. This will be referred to as a "distribution." In 1011

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Bestimmung der Reihenfolge der Aminosäuren am Carboxylende des Tabakmosaikvirus durch Hydrazinspaltung

Braunitzer

1955

Chem. Ber.

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Nr. 12/1955]Braunitzer 2025 ~-l-[2.4.6-Trimethyl-benzoyl]-~-galaktose (p-l-Mesitoyl-D-galaktose):Die Verseifung erfolgte wie bei der entsprechenden D-Glucose-Verbindung beschrieben. Die P-l-Mesitoyl-D-gelaktose kristallisiert &us warmem Akohol ohne Zusatz von Ather und Petroliither. Ausb. aus 15 g Tetraacetyl-P-l-mesitoyl-D-gahktose 9.2 g P-l-Mesitoyl-D-galaktose (93% d. Th.). Schmp. 153'; [a]g: +28.7' (Wmser, c=0.8). C18H220, (326.3) Ber. C 58.88 H6.80 Gef. C 58.64 H6.73Anhydrisierung d e r P-l-Mesitoyl-D-galaktose: Die Anhydrisierung wurde, wie bei der Glucoseverbindung beschrieben, durchgefiihrt. Aus 3.22 g Mesitoyl-n-galaktose in 500 ccm Wwser (a. mlao Lijsung) wurden 700 ccm Lijsung von [a], : -6.5" erhalten, entspr. a. 1 g D-Galaktosan.Die Aufarbeitung ergab 1.19 g (74.5% d. Th.) krist. D-Galaktosan <1.5> <1.6>. [a]g: -19.9' (Wasser, c = 1.1). Umkristallisiert ausAthano1, Phtten vom Schmp. 226". [a]g : -21.8" (Wasser, c=1.2). Der Misch-Schmp. mit authentischem D-Gahktosan zeigte keine Depression. Mit Acetanhydridj€'yridin acetyliert und wie iiblich aufgearbeitet, wird D -G a l a kt o s a n -t r i a c e t a t vom SchIpp. 74" und [a]%: -5.6" (Chlf., c=1.4) erhalten.' Behandlung von ( 3 -1 -Benzoyl-D-glucose m i t Alkali: p -1 -Benzoyl-D-glucose wurde nach Z e r v d o ) dargestellt. Schmp. 196", [als: -26.7' (WcLsser, c=O.9). Die Substanz erfiihrt, in Wasser gelost, bei Zimmertemperatur i m Laufe von 24 Stdn. keine Drehwertsiinderung. In rrho NaOH erfolgt mgenblicklich starke Verschiebung nach rechts utid spiiter langsamer Abfall bis auf 0' in 24 Stdn. (8. Tafel). Bei 100" geht der Drehwert in wenigen Minuten auf 0' zuriick. Durch eine wie oben mit Austauscher beschickte heizbare Siiule, Inhalt 10 ccm Amberlite IRA400, liiBt man bei 50" 100 ccrn Warner, in dem 0.2760g p-1-Benzoyl-Dglucose gelost sind, mit einer Geschwindigkeit von rd. 1 ccm/Min. hindurcMieBen. Die abhufende Lijsung wird, wie oben beschrieben, gesammelt und der Drehwert M i m m t . Es treten neben Fraktionen ohne opt. Drehung nur positiv drehende Fmktionen auf. Sie werden gesammelt, i. Vak. konzentriert und das erhaltene Produkt papierchromatographisch untersucht. Es konnten lediglich Glucose und daneben etwas Mannose und Fructose chromatogmphisch nachgewiesen werden.. Gerhard Braunitzer: Bestimmung der Reihenfolge der Aminosiiuren am Carboxylende des Tabakmosaikvirus durch HydrazinspaltungDie Methode zur Bestimmung des C-terminden Restes einer Peptidkette nach Akabori wurde untersucht; die besten Durchfiihrungsbedingungen werden angegeben. Modellversuche ergaben eine gute Bestiindigkeit der Aminosiiuren gegeniiber Hydmzin. Arginin wird zu Ornithin abgebaut. Die Bestimmung der C-terminalen Sequenz durch kurzzeitige Einwirkung von Hydrazin auf das native TMY ergab, daB siimtliche Peptidketten dieselbe C-terminale Sequenz : Prolin -Alanin-Threonin besitzen. Dieass Ergebnis h e nach Einwirkung von Carboqpeptidase auf das native Virus durch totale und partielle Spltung mit Hydrrtzin bestiitigt. Von Akabori und M3tarbb.l) wurde eine Methode zur Best...

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On the Structure of Lysozyme

Cited by 20 publications

References 0 publications

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹

Statistical Correlation of Protein and Ribonucleic Acid Composition

Bestimmung der Reihenfolge der Aminosäuren am Carboxylende des Tabakmosaikvirus durch Hydrazinspaltung

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On the Structure of Lysozyme

Cited by 20 publications

References 0 publications

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis1

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis1

Statistical Correlation of Protein and Ribonucleic Acid Composition

Bestimmung der Reihenfolge der Aminosäuren am Carboxylende des Tabakmosaikvirus durch Hydrazinspaltung

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Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹

Determination of C-Terminal Amino Acids and Peptides by Hydrazinolysis¹