scholarly journals Chemical studies on the cysteine and terminal peptides in tryptic digests of actin

1968 ◽  
Vol 110 (2) ◽  
pp. 207-216 ◽  
Author(s):  
P. Johnson ◽  
S V Perry
Keyword(s):  
Tryptic Peptide ◽  
Polypeptide Chain ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Carboxypeptidase A ◽  
Single Polypeptide Chain ◽  
Chemical Studies ◽  
Single Polypeptide ◽  
Peptide Maps ◽  
Chemical Evidence

1. On exhaustive digestion of carboxymethylated actin in 6m-urea solutions with carboxypeptidase A, 1 mole of phenylalanine was liberated/43000g. of protein. At a lower urea concentration and in the absence of urea, carboxymethyl-cysteine (CMCys) was also liberated. 2. Three cysteine-containing peptides were identified by the study of peptide ‘maps’ of tryptic digests of actin treated with thiol reagents. 3. The three peptides, each containing one residue of CMCys, were isolated from tryptic digests of carboxymethylated actin by ion-exchange chromatography. 4. One of these peptides was possibly the N-terminal peptide and contained about 17–18 residues; another was CMCys-Asp-Ile-Asp-Ile-Arg; the other, CMCys-Phe, was the C-terminal tryptic peptide. 5. The chemical evidence suggests that the actin molecule consists of a single polypeptide chain of molecular weight about 44000.

scholarly journals Hepatic microsomal epoxide hydrase. Chemical evidence for a single polypeptide chain.

1979 ◽  
Vol 254 (14) ◽  
pp. 6240-6243 ◽  
Author(s):  
G C DuBois ◽  
E Appella ◽  
R Armstrong ◽  
W Levin ◽  
A Y Lu ◽  
...  
Keyword(s):  
Polypeptide Chain ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Chemical Evidence

scholarly journals The purification and some properties of rusticyanin, a blue copper protein involved in iron(II) oxidation from Thiobacillus ferro-oxidans

1978 ◽  
Vol 174 (2) ◽  
pp. 497-502 ◽  
Author(s):  
J C Cox ◽  
D H Boxer
Keyword(s):  
Polypeptide Chain ◽  
Iron Oxidation ◽  
Exchange Chromatography ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Optical Absorbance ◽  
Single Polypeptide Chain ◽  
Arginine Residues ◽  
Single Polypeptide

The ‘blue’ copper-containing protein rusticyanin was purified to homogeneity from cells of the chemolithotrophic bacterium Thiobacillus ferro-oxidans by (NH4)SO4 fractionation and ion-exchange chromatography. The protein, which is stable at low pH, consists of a single polypeptide chain of mol. wt. 16500 and possesses 0.79 (+/- 0.28)g-atom of Cu/mol. The protein, which does not contain arginine residues, has optical absorbance maxima at 287, 450, 597 and 750 nm and is generally similar to azurin. The isolated protein is reduced directly by Fe2+ with a 1:1 stoicheiometry to Cu. On reduction by Fe2+ the absorption peaks at 450, 597 and 750 nm are abolished, with the appearance of a new absorption band at 320 nm. The results obtained are consistent with rusticyanin being the initial acceptor of electrons from Fe2+ during respiratory iron oxidation.

scholarly journals Evidence for the amino acid sequence of porcine pancreatic elastase

1973 ◽  
Vol 131 (4) ◽  
pp. 643-675 ◽  
Author(s):  
David M. Shotton ◽  
Brian S. Hartley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Pancreatic Elastase ◽  
Single Polypeptide Chain ◽  
Chemical Studies ◽  
Lending Library ◽  
Porcine Pancreatic Elastase ◽  
Single Polypeptide

The preparation and purification of tryptic peptides from aminoethylated Dip-elastase and [14C]carboxymethylated Dip-elastase, and of peptic peptides from native elastase is described. A summary of the results of chemical studies used to elucidate the amino acid sequence of these peptides is presented. Full details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50016 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 1–20. These results, together with those from previously published papers, are used to establish the complete amino acid sequence of elastase, which is a single polypeptide chain of 240 residues, molecular weight 25900, containing four disulphide bridges.

Preparation and properties of β-casein from buffalo's milk

1975 ◽  
Vol 42 (1) ◽  
pp. 163-167 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
Safinaz El-Shibiny
Keyword(s):  
Gel Electrophoresis ◽  
Tryptic Peptide ◽  
Polypeptide Chain ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Terminal Sequence ◽  
Single Polypeptide Chain ◽  
End Groups ◽  
Starch Gel ◽  
Single Polypeptide

Summaryβ-Casein from individual buffalo's milk was found to be homogeneous by starch-gel electrophoresis. β-Casein was separated from buffalo's milk by the method of Warner (1944) and purified by DEAE-cellulose chromatography.Buffalo β-casein possesses identical end-groups to those of cow β-casein; namely N-terminal arginine and assuming a single polypeptide chain a possible C-terminal sequence of Ile-Ile-Val. However, the amino-acid composition and the tryptic peptide patterns of the 2 proteins are not the same.

THE PHYSIOLOGICAL ANTITHROMBIN (BETA) VARIANT WITH INCREASED HEPARIN AFFINITY LACKS CARBOHYDRATE AT ASN 135

1987 ◽  
Author(s):  
S O Brennan ◽  
P M George ◽  
R W Carrel ◽  
R Jordan
Keyword(s):  
Polypeptide Chain ◽  
Molecular Model ◽  
Terminal Sequence ◽  
Single Polypeptide Chain ◽  
Attachment Sites ◽  
At Iii ◽  
Single Polypeptide ◽  
Heparin Affinity ◽  
Peptide Maps ◽  
Variant Identification

Some 10% of the antithrombin fromnormal human plasma can be isolated onthe basis of its higher affinity forheparin Sepharose. Not only does this ATIII beta have a higher heparinaffinity, but it is also less negatively charged and has a lower molecular weight than normal AT-III alpha.Neuraminidase and Endo F treatment suggest the loss of a single carbohydrate sidechain from beta AT-III (Peterson and Blackburn. J Biol Chem 1985,260, 610)Antithrombin has a single polypeptide chain with biantennary carbohydrate attachment sites at asparagines 96, 135, 155 and 172. The 25 kDA CNBr fragment of AT-III alpha (residues 104-251) runs at 22.5kDa in the case of AT-III beta yet they have the same N and C-terminal sequence. Tryptic peptide maps of theseCNBr fragments showed that a single neutral (glyco) peptide, Lys-Ala-Asn⋆-Lys was missing from AT-III beta and replaced by twobasic peptides, Lys, Ala, Asn, Lys and Ala, Asn, Lys; indicating the absence of an oligosaccharide sidechainon asparagine 135. This was confirmed by chromatography of tryptic peptides on Con A-Sepharose followed by mapping of the bound and unbound fractions. There were two new unbound peptides (Lys, Ala, Asn, Lys and Ala, Asn, Lys) in AT-III beta. The corresponding peptide Lys-Ala-Asn⋆-Lys was the only peptide missing from the bound glycopeptide fraction.The absence of carbohydrate at Asn 135 explains the increased heparinaffinity of beta AT-III as on the molecular model this oligosaccharide forms a negative and bulky shell on the perimeter of the positive bindingsite centred on Arg 47.Whether the loss of the sidechain is due to circulatory removal is not known but a recent variant identification confirmsthat it may alternatively be due to failure of attachment at the time ofsynthesis. Potentially the loss or modification of oligosaccharide 135 provides another level of control of coagulation by altering the avidity of AT-III for thrombin when heparin activation is suboptimal.

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres

scholarly journals Identification of Igh-C-linked determinants on suppressor T cell hybrids and factors specific for L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT).

1985 ◽  
Vol 162 (3) ◽  
pp. 1044-1059 ◽  
Author(s):  
C M Sorensen ◽  
R J Hayashi ◽  
C W Pierce
Keyword(s):  
T Cells ◽  
T Cell ◽  
Polypeptide Chain ◽  
Spleen Cells ◽  
Suppressor T Cell ◽  
Cell Hybrids ◽  
Single Polypeptide Chain ◽  
Functional Classes ◽  
Single Polypeptide ◽  
Ig Allotype

Hyperimmunization of BALB/c mice with concanavalin A-stimulated blasts from the Ig allotype-congenic strain, C.B20, results in the production of antibodies reactive with T cells in an allotype-restricted manner. Spleen cells from these hyperimmune BALB/c mice were used to generate a panel of hybridomas that secrete monoclonal antibodies, reactive, in an allotype-restricted manner, exclusively with T cells subpopulations, and in particular, reactive with suppressor T cell hybridomas and their secreted soluble factors. Two functional classes of antibodies were identified: those that react with single polypeptide-chain suppressor T cell factors (TsF1) and the suppressor T cell hybridomas that produce such factors, and those that react with two polypeptide-chain suppressor T cell factors (TsF2) and their corresponding suppressor T cell hybridomas. These two classes of antibody were used to isolate molecules from the membranes of the respective suppressor T cell hybrids that are functionally and structurally related to the secreted suppressor T cell factors, suggesting a receptor function for these molecules.

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