scholarly journals The Possibility of Common Amino Acid Sequences in High-Sulphur Protein Fractions from Wool

1969 ◽  
Vol 22 (5) ◽  
pp. 1197 ◽  
Author(s):  
RL Darskus ◽  
JM Gillespie ◽  
H Lindley
Keyword(s):  
Amino Acid ◽  
High Voltage ◽  
Paper Electrophoresis ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
Protein Fractions ◽  
Common Amino Acid ◽  
Amino Acid Compositions ◽  
Merino Wool ◽  
Derivatives Of

S-Carboxymethyl derivatives of the high-sulphur components of reduced Merino wool have been subdivided by chromatography into 17 fractions, the amino acid compositions of which are reported. Tryptic, chymotryptic, and thermolysin digests of each fraction have been studied by high-voltage paper electrophoresis at pH 3�5 and 6�5. The results suggest that the high-sulphur proteins consist of families of proteins probably containing common structural features. Evidence is presented that the heterogeneity of high-sulphur proteins is not artefactual.

Isolation and characterization of some novel genes of the apolipoprotein A-I family in Japanese eel, Anguilla japonica

2011 ◽  
Vol 6 (4) ◽  
pp. 545-557 ◽  
Author(s):  
Malay Choudhury ◽  
Takahiro Oku ◽  
Shoji Yamada ◽  
Masaharu Komatsu ◽  
Keita Kudoh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Consensus Sequence ◽  
Structural Features ◽  
Lipid Binding ◽  
Japanese Eel ◽  
Amino Acid Sequences ◽  
Novel Genes ◽  
Isolation And Characterization

AbstractApolipoproteins such as apolipoprotein (apo) A-I, apoA-IV, and apoE are lipid binding proteins synthesized mainly in the liver and the intestine and play an important role in the transfer of exogenous or endogenous lipids through the circulatory system. To investigate the mechanism of lipid transport in fish, we have isolated some novel genes of the apoA-I family, apoIA-I (apoA-I isoform) 1–11, from Japanese eel by PCR amplification. Some of the isolated genes of apoIA-I corresponded to 28kDa-1 cDNAs which had already been deposited into the database and encoded an apolipoprotein with molecular weight of 28 kDa in the LDL, whereas others seemed to be novel genes. The structural organization of all apoIA-Is consisted of four exons separated by three introns. ApoIA-I10 had a total length of 3232 bp, whereas other genes except for apoIA-I9 ranged from 1280 to 1441 bp. The sequences of apoIA-Is at the exon-intron junctions were mostly consistent with the consensus sequence (GT/AG) at exon-intron boundaries, whereas the sequences of 3′ splice acceptor in intron 1 of apoIA-I1-7 were (AC) but not (AG). The deduced amino acid sequences of all apoIA-Is contained a putative signal peptide and a propeptide of 17 and 5 amino acid residues, respectively. The mature proteins of apoIA-I1-3, 7, and 8 consisted of 237 amino acids, whereas those of apoIA-I4-6 consisted of 239 amino acids. The mature apoIA-I10 sequence showed 65% identity to amino acid sequence of apoIA-I11 which was associated with an apolipoprotein with molecular weight of 23 kDa in the VLDL. All these mature apoIA-I sequences satisfied the common structural features depicted for the exchangeable apolipoproteins such as apoA-I, apoA-IV, and apoE but apoIA-I11 lacked internal repeats 7, 8, and 9 when compared with other members of apoA-I family. Phylogenetic analysis showed that these novel apoIA-Is isolated from Japanese eel were much closer to apoA-I than apoA-IV and apoE, suggesting new members of the apoA-I family.

Structural studies of hemoglobin from two flightless birds, ostrich and turkey: insights into their differing oxygen-binding properties

2021 ◽  
Vol 77 (5) ◽  
pp. 690-702
Author(s):  
Pandian Ramesh ◽  
Selvarajan Sigamani Sundaresan ◽  
Nagaraj Shobana ◽  
Thangaraj Vinuchakkaravarthy ◽  
Kandasamy Sivakumar ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structural Features ◽  
Crystal Structure Analysis ◽  
Oxygen Molecule ◽  
Amino Acid Sequences ◽  
Physical Parameters ◽  
Oxygen Binding ◽  
Binding Properties ◽  
Form Analysis ◽  
Inverse Transition

Crystal structures of hemoglobin (Hb) from two flightless birds, ostrich (Struthio camelus) and turkey (Meleagris gallopova), were determined. The ostrich Hb structure was solved to a resolution of 2.22 Å, whereas two forms of turkey Hb were solved to resolutions of 1.66 Å (turkey monoclinic structure; TMS) and 1.39 Å (turkey orthorhombic structure; TOS). Comparison of the amino-acid sequences of ostrich and turkey Hb with those from other avian species revealed no difference in the number of charged residues, but variations were observed in the numbers of hydrophobic and polar residues. Amino-acid-composition-based computation of various physical parameters, in particular their lower inverse transition temperatures and higher average hydrophobicities, indicated that the structures of ostrich and turkey Hb are likely to be highly ordered when compared with other avian Hbs. From the crystal structure analysis, the liganded state of ostrich Hb was confirmed by the presence of an oxygen molecule between the Fe atom and the proximal histidine residue in all four heme regions. In turkey Hb (both TMS and TOS), a water molecule was bound instead of an oxygen molecule in all four heme regions, thus confirming that they assumed the aqua-met form. Analysis of tertiary- and quaternary-structural features led to the conclusion that ostrich oxy Hb and turkey aqua-met Hb adopt the R-/RH-state conformation.

Subunit II (b') and Not Subunit I (b) of Photosynthetic ATP Synthases is Equivalent to Subunit b of the ATP Synthases from Nonphotosynthetic Eubacteria. Evidence for a New Assignment of b-Type F0 Subunits

1997 ◽  
Vol 52 (11-12) ◽  
pp. 789-798 ◽  
Author(s):  
Hans-Jürgen Tiburzy ◽  
Richard J. Berzborn
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Structural Feature ◽  
Atp Synthase ◽  
Primary Structure ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
E Coli ◽  
Subunit B ◽  
Atp Synthases

Abstract Subunit I of chloroplast ATP synthase is reviewed until now to be equivalent to subunit b of Escherichia coli ATP synthase, whereas subunit II is suggested to be an additional subunit in photosynthetic ATP synthases lacking a counterpart in E. coli. After publication of some sequences of subunits II a revision of this assignment is necessary. Based on the analysis of 51 amino acid sequences of b-type subunits concerning similarities in primary structure, iso­electric point and a discovered discontinuous structural feature, our data provide evidence that chloroplast subunit II (subunit b' of photosynthetic eubacteria) and not chloroplast subunit I (subunit b of photosynthetic eubacteria) is the equivalent of subunit b of nonphoto­ synthetic eubacteria, and therefore does have a counterpart in e.g. E. coli. In consequence, structural features essential for function should be looked for on subunit II (b').

scholarly journals The sequence of amino acids in insulin isolated from islet tissue of the cod (Gadus callarias)

1968 ◽  
Vol 110 (2) ◽  
pp. 289-296 ◽  
Author(s):  
K. B. M. Reid ◽  
P T Grant ◽  
A. Youngson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Small Peptides ◽  
Islet Tissue ◽  
Complete Digestion ◽  
The Individual ◽  
Derivatives Of

1. S-Aminoethylcysteinyl derivatives of the A and B chains of cod insulin were prepared from the individual S-sulpho chains. 2. Studies on small peptides derived from the S-aminoethylated peptide chains by treatment with trypsin allowed the amino acid sequences in the region of the cysteinyl residues of the A and B peptide chains to be defined. 3. The six amide groups in cod insulin were located by complete digestion of small peptides from the A and B chains with aminopeptidase followed by amino acid analyses. 4. The results, together with previous studies on the oxidized A and B chains, define the sequences of the 51 amino acids that constitute cod insulin.

SEPARATION OF THE PROTEIN CONSTITUENTS OF THE LARVAL DIETS OF THE HONEYBEE BY CONTINUOUS PAPER ELECTROPHORESIS

1959 ◽  
Vol 37 (6) ◽  
pp. 957-964 ◽  
Author(s):  
J. E. J. Habowsky ◽  
R. W. Shuel
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Free Amino Acid ◽  
Aspartic Acid ◽  
Free Amino ◽  
Royal Jelly ◽  
Paper Electrophoresis ◽  
Protein Fractions ◽  
Electrophoretic Patterns

The protein constituents of the larval diets of queen and worker honeybees were separated by continuous paper electrophoresis. The electrophoretic patterns of royal jelly of any age and the early worker diet were similar and comprised five ninhydrin-reactive bands or fractions. Fraction 1 (nearest the cathode) contained lysine as a free amino acid. Fractions 3 and 4 appeared to be complex polypeptides. Alanine, asparagine, aspartic acid, glutamic acid, glycine, histidine, isoleucine and/or leucine, lysine, phenylalanine, threonine, tyrosine, valine, and an unidentified substance were found in chromatograms of the acid hydrolyzate of fraction 3; the hydrolyzate of fraction 4 contained the same amino acids except for threonine. Fractions 2 and 5 were not characterized. Electrophoresis of the diet of worker larvae older than 3 days showed a pronounced fading of all bands, attributable to the dilution of the solids by the addition of honey which occurs at this time. There appeared to be no qualitative differences between the protein fractions of royal jelly and worker diet which would account for the differentiation of female honeybees into queens and workers. The decrease with age in the percentage of protein in the worker diet may be significant.

INCORPORATION OF C14INTO BACTERIAL PEPTIDES

1958 ◽  
Vol 4 (6) ◽  
pp. 633-648 ◽  
Author(s):  
G. E. Connell ◽  
R. W. Watson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
High Voltage ◽  
Basic Amino Acid ◽  
Paper Electrophoresis ◽  
Total Radioactivity ◽  
Before And After ◽  
Basic Peptides ◽  
Peptide Fractions

Alcoholic extracts of log-phase cells of Pseudomonas hydrophila grown on glucose as the sole carbon source were concentrated, extracted with ether, and dialyzed. After fractionation of the permeates by high voltage paper electrophoresis, five to seven ninhydrin-positive acidic, one neutral, and several basic bands appeared. As many as seven ninhydrin-positive basic bands have been found in some preparations, although they have been absent in others. Photometric analyses on eluates before and after acid hydrolysis indicated the presence of acidic, neutral, and basic peptides. Amino acid compositions of 28 of these peptides, separated by a combination of high voltage paper electrophoresis and paper chromatography, included all of the amino acids commonly found in proteins. Elution of acidic, neutral, and basic amino acid and peptide fractions from C14-labelled cells was followed by measurement of total and specific radioactivities in carboxyl-C before and after acid hydrolysis. Total radioactivity was highest in proteins even 1 minute after addition of the isotope to a log-phase culture. Specific radioactivities, plotted against time, gave parallel hyperbolic curves with peptides below the curve for amino acids and with proteins still lower and almost linear. The evidence suggests rapid synthesis of peptides from amino acids.

scholarly journals Structural analyses of the deduced amino acid sequences of a novel type heme–copper terminal oxidase, cytochrome aco3, from alkalophilic Bacillus YN-2000

2001 ◽  
Vol 47 (12) ◽  
pp. 1075-1081 ◽  
Author(s):  
Kimitoshi Denda ◽  
Akira Oshima ◽  
Yoshihiro Fukumori
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Basic Amino Acid ◽  
Structural Features ◽  
Thermophilic Bacterium ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Bacterium Bacillus ◽  
Alkalophilic Bacillus

Cytochrome aco3 from a facultatively alkalophilic bacterium, Bacillus YN-2000, was found to be alkaline- and heat-tolerant. To better understand the structural features of Bacillus YN-2000 cytochrome aco3, the gene encoding this enzyme was cloned and sequenced. Nucleotide sequence analyses of the region neighboring the acoI (subunit I) gene revealed that the acoII (subunit II) and acoIII (subunit III) genes were concomitantly clustered upstream and downstream of the acoI gene, respectively, forming an operon with transcriptional polarity. The deduced amino acid sequence of subunit I was highly similar to that of cytochrome caa3 from thermophilic bacterium Bacillus PS3 in which the heme a3 could be replaced with heme o. Furthermore, a marked paucity of basic amino acid residues was found in the cytochrome c-binding subunit II, which might be a result of the adaptation to a highly alkaline external milieu.Key words: cytochrome c oxidase, alkalophile, thermostability, heme o, Bacilli.

scholarly journals Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool

1967 ◽  
Vol 102 (3) ◽  
pp. 801-814 ◽  
Author(s):  
M. C. Corfield ◽  
J. C. Fletcher ◽  
A. Robson
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Protein Fraction ◽  
Exchange Resin ◽  
Cation Exchange Resin ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
Tryptic Digest ◽  
Parent Protein ◽  
Wool Proteins

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of the peptides in the digest present in the largest amounts have been determined. 4. The amino acid sequences of 38 of these have been completely elucidated and those of six others partially derived. 5. These findings indicate that the parent protein in wool from which the protein fraction U.S.3 is derived has a minimum molecular weight of 74000. 6. The structures of wool proteins are discussed in the light of the peptide sequences determined, and, in particular, of those sequences in fraction U.S.3 that could not be elucidated.

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