TERMINAL AMINO ACIDS OF EGG YOLK LIPOPROTEINS

1961 ◽  
Vol 39 (6) ◽  
pp. 1075-1084 ◽  
Author(s):  
J. M. Neelin ◽  
W. H. Cook
Keyword(s):  
Amino Acids ◽  
Average Molecular Weight ◽  
Egg Yolk ◽  
Water Soluble ◽  
Terminal Amino Acid ◽  
Physical Measurements ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Protein Moiety ◽  
Egg Yolk Lipoproteins

The N-terminal amino acids of the two lipovitellins and lipovitellenin of egg yolk have been determined. α-Lipovitellin and β-lipovitellin were separated by chromatography on hydroxyapatite but the lipovitellenin in the low-density fraction did not yield stable and reproducible chromatographic components. The major N-terminal amino acids recovered as dinitrophenyl derivatives from all three fractions were arginine and lysine. Further purification removed several minor components, but tyrosine and serine remained in vitellin, and alanine and serine in vitellenin. The principal C-terminal amino acid of vitellenin was glutamic acid. Arginine appeared to be the chief N-terminal residue but difficulty in purifying the water-soluble dinitrophenyl-amino acids led to highly variable yields; thus the total calculated amounts of terminal amino acids ranged from 9 to 35 micromoles per gram of protein. At least two polypeptide chains are indicated, with an average molecular weight less than the size of the total protein moiety of the parent lipoprotein. This is consistent with reported physical measurements in formic acid. The three lipoprotein fractions are indistinguishable on the basis of their terminal amino acids.

N-TERMINAL AMINO ACIDS OF THE PROTEINS OF THE FLOATING FRACTION OF EGG YOLK

1958 ◽  
Vol 36 (9) ◽  
pp. 951-952 ◽  
Author(s):  
David B. Smith ◽  
K. J. Turner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Primary Structure ◽  
Egg Yolk ◽  
Minor Components ◽  
Terminal Amino Acid ◽  
Hen’S Egg ◽  
Terminal Amino

Lysine is the major N-terminal amino acid of both the soluble and insoluble fractions of the floating lipoprotein of hen's egg yolk, which suggests a common primary structure. Several minor components are also present in both fractions.

N-TERMINAL AMINO ACIDS OF THE PROTEINS OF THE FLOATING FRACTION OF EGG YOLK

1958 ◽  
Vol 36 (1) ◽  
pp. 951-952 ◽  
Author(s):  
David B. Smith ◽  
K. J. Turner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Primary Structure ◽  
Egg Yolk ◽  
Minor Components ◽  
Terminal Amino Acid ◽  
Hen’S Egg ◽  
Terminal Amino

Lysine is the major N-terminal amino acid of both the soluble and insoluble fractions of the floating lipoprotein of hen's egg yolk, which suggests a common primary structure. Several minor components are also present in both fractions.

A COMPARISON OF PHOSVITINS PREPARED FROM HEN'S SERUM AND FROM HEN'S EGG YOLK

1961 ◽  
Vol 39 (1) ◽  
pp. 109-117 ◽  
Author(s):  
Chi-Ching Mok ◽  
W. G. Martin ◽  
R. H. Common
Keyword(s):  
Molecular Weight ◽  
Average Molecular Weight ◽  
Egg Yolk ◽  
Terminal Amino Acid ◽  
Weight Average Molecular Weight ◽  
Sedimentation Constant ◽  
Hen’S Egg ◽  
Zone Electrophoresis ◽  
Terminal Amino ◽  
Tryptophan Content

A phosvitin has been prepared from the serum of estrogenized laying hens and partially characterized on the basis of its contents of N (12.3%), P (10.1%), serine (31.0%), and tryptophan (0.56%). Examination of this serum phosvitin and a yolk phosvitin preparation for N-terminal groups yielded identical chromatographic patterns. Alanine was the major N-terminal amino acid with minor amounts of N-terminal lysine. The sedimentation constant [Formula: see text], weight-average molecular weight 4.2 × 104(Archibald method), and number-average molecular weight 4.0 × 104(calculated from the tryptophan content) of the serum phosvitin were similar to those of the phosvitin prepared from egg yolk by the same preparative technique. The two preparations behaved similarly when subjected to zone electrophoresis on paper.Zone electrophoretic evidence is submitted for the presence of phosvitin in the supernatant from dilution precipitation of crude lipophosphoprotein from laying hen's serum as well as in the precipitate itself.

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Amide Nitrogen ◽  
Acetylneuraminic Acid ◽  
Hen’S Egg ◽  
Terminal Amino ◽  
Protein Moiety

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

Existence of Common Antigenic Determinants in the Aα, Bβ and γ Chains of Some Mammalian Fibrinogens.

1979 ◽  
Author(s):  
C.S. Cierniewski
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Antigenic Determinants ◽  
Terminal Amino Acid ◽  
Human Fibrinogen ◽  
Passive Hemagglutination ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

Polypeptide chains Aα, Bβ and γ of porcine fibrinogen were isolated by preparative SDS polyacrylamide gel electrophoresis. Their purity was estimated by electrophoresis in polyacrylamide gel, amino acid composition and N-terminal amino acid analyses. Antisera to the pig polypeptide chains were produced in rabbits and they were employed in immunological comparative studies of porcine, bovine, human and duck fibrinogens. Antisera to the pig Aα chain showed in gel immunodiffusion and passive hemagglutination a strong cross-reaction with porcine, bovine and human fibrinogens. Antisera to the pig βB and γ chains cross-reacted only with porcine and bovine fibrinogens but they did not recognize human fibrinogen, The reaction of antiγ antisera was detectable only by passive hemagglutination test. In all cases antigenic similarity of the analyzed fibrinogens was mainly related to antigenic determinants of the Aα, Bβ and γ chains exposed on the intact fibrinogen molecule. None of analyzed antisera reacted with duck fibrinogen.

Studies on Nα-acylated proteins: The N-terminal sequences of two muscle enolases

1985 ◽  
Vol 5 (10-11) ◽  
pp. 847-854 ◽  
Author(s):  
Christopher C. Q. Chin ◽  
Finn Wold
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Coho Salmon ◽  
Standard Procedure ◽  
Exchange Chromatography ◽  
Rabbit Muscle ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Acylated Proteins

A standard procedure for the identification of the N-terminal amino acid in Nα-acylated proteins has been developed. After exhaustive proteolysis, the amino acids with blocked α-amino groups are separated from positively charged, free amino acids by ion exchange chromatography and subjected to digestion with acylase I. Amino acid analysis before and after the acylase treatment identifies the blocked N-terminal amino acid. A survey of acylamino acid substrates showed that acytase will liberate all the common amino acids except Asp, Cys or Pro from their N-acetyl- and N-butyryl derivatives, and will also catalyze the hydrolysis of N-formyl-Met and N-myristyl-Val. Thus, the procedure cannot identify acylated Asp, Cys or Pro, nor, because of the ion exchange step, Nα-acyl-derivatives of Arg, Lys or His. Whenever the protease treatment releases free acylamino acids, the remaining amino acids should be detected. When applied to several proteins, the procedure confirmed known N-terminal acylamino acids and identified acyl-Ser in enolases from chum and coho salmon muscle and in pyruvate kinase from rabbit muscle, and acyl-Thr in phosphofructokinase from rabbit muscle. The protease-acylase assay has been used to identify blocked peptides from CNBr- or protease-treated proteins. When such peptides were treated with 1n HCl at 110° for 10 min, sufficient yields of deacylated, mostly intact, peptide were obtained to permit direct automatic sequencing. The N-terminal sequences of rabbit muscle and coho salmon enolase were determined in this way and are compared to each other and to the sequence of yeast enolase.

scholarly journals Determination of Peptide Contact Points in the Human Angiotensin II Type I Receptor (AT1) with Photosensitive Analogs of Angiotensin II

1999 ◽  
Vol 13 (4) ◽  
pp. 578-586 ◽  
Author(s):  
Stéphane A. Laporte ◽  
Antony A. Boucard ◽  
Guy Servant ◽  
Gaétan Guillemette ◽  
Richard Leduc ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Angiotensin Ii ◽  
Transmembrane Domain ◽  
At1 Receptor ◽  
High Yield ◽  
Type I ◽  
Terminal Amino Acid ◽  
Contact Points ◽  
Terminal Amino

Abstract To identify ligand-binding domains of Angiotensin II (AngII) type 1 receptor (AT1), two different radiolabeled photoreactive AngII analogs were prepared by replacing either the first or the last amino acid of the octapeptide by p-benzoyl-l-phenylalanine (Bpa). High yield, specific labeling of the AT1 receptor was obtained with the 125I-[Sar1,Bpa8]AngII analog. Digestion of the covalent 125I-[Sar1,Bpa8]AngII-AT1 complex with V8 protease generated two major fragments of 15.8 kDa and 17.8 kDa, as determined by SDS-PAGE. Treatment of the[ Sar1,Bpa8]AngII-AT1 complex with cyanogen bromide produced a major fragment of 7.5 kDa which, upon further digestion with endoproteinase Lys-C, generated a fragment of 3.6 kDa. Since the 7.5-kDa fragment was sensitive to hydrolysis by 2-nitro-5-thiocyanobenzoic acid, we circumscribed the labeling site of 125I-[Sar1,Bpa8]AngII within amino acids 285 and 295 of the AT1 receptor. When the AT1 receptor was photolabeled with 125I-[Bpa1]AngII, a poor incorporation yield was obtained. Cleavage of the labeled receptor with endoproteinase Lys-C produced a glycopeptide of 31 kDa, which upon deglycosylation showed an apparent molecular mass of 7.5 kDa, delimiting the labeling site of 125I-[Bpa1]AngII within amino acids 147 and 199 of the AT1 receptor. CNBr digestion of the hAT1 I165M mutant receptor narrowed down the labeling site to the fragment 166–199. Taken together, these results indicate that the seventh transmembrane domain of the AT1 receptor interacts strongly with the C-terminal amino acid of[ Sar1, Bpa8]AngII, whereas the N-terminal amino acid of[ Bpa1]AngII interacts with the second extracellular loop of the AT1 receptor.

Nuclear Magnetic Resonance Studies of Phenylthiohydantoin Amino Acids

1975 ◽  
Vol 53 (9) ◽  
pp. 1005-1009 ◽  
Author(s):  
C. S. Tsai ◽  
N. L. Fraser ◽  
H. Avdovich ◽  
J. P. Farant
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Amino Acid ◽  
Magnetic Resonance ◽  
Diagnostic Purpose ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Magnetic Resonance Studies ◽  
Terminal Amino ◽  
Derivatives Of

Proton magnetic spectra of 3-phenyl-2-thiohydantoin derivatives of common amino acids in deuterated dimethyl sulfoxide were recorded. Spectral data pertaining to characteristic protons for diagnostic purpose were compiled. Their application to the N-terminal amino acid analysis of peptide by Edman degradation was examined.

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