THE HISTONES OF CHICKEN ERYTHROCYTE NUCLEI

1964 ◽  
Vol 42 (12) ◽  
pp. 1743-1752 ◽  
Author(s):  
J. M. Neelin ◽  
P. X. Callahan ◽  
D. C. Lamb ◽  
K. Murray
Keyword(s):  
Amino Acid ◽  
Amino Acid Content ◽  
Exchange Chromatography ◽  
Chicken Erythrocyte ◽  
Terminal Amino Acid ◽  
Electrophoretic Behavior ◽  
Calf Thymus ◽  
Somatic Tissues ◽  
Starch Gel ◽  
Terminal Amino

Five fractions of chicken erythrocyte histone have been obtained by ion-exchange chromatography, and compared with calf thymus histone fractions in amino acid composition, electrophoretic behavior in starch gel, N-terminal amino acid content, and fingerprint of tryptic peptides. A major erythrocyte histone fraction, rich in both lysine and arginine, as well as serine, was peculiar to these singular cells, and appeared to replace the "arginine-rich" histone of other somatic tissues. In contrast, the other four erythrocyte histone fractions were closely similar in kind to their chromatographic counterparts in calf tissues, despite some differences in number and yield. The occurrence of this unusual histone may be related to the limited biosynthetic capacities of these cells with highly differentiated nuclei.

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 Isolation of four forms of acetone-induced cytochrome P-450 in chicken liver by h.p.l.c. and their enzymic characterization

1990 ◽  
Vol 269 (1) ◽  
pp. 85-91 ◽  
Author(s):  
J F Sinclair ◽  
S Wood ◽  
L Lambrecht ◽  
N Gorman ◽  
L Mende-Mueller ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Chicken Liver ◽  
Terminal Amino Acid ◽  
Catalytic Activities ◽  
Terminal Amino ◽  
Cytochrome P 450 ◽  
Terminal Amino Acid Sequence

The purpose of this study was to purify and characterize the forms of cytochrome P-450 induced in chicken liver by acetone or ethanol. Using high performance liquid ion-exchange chromatography, we were able to isolate at least four different forms of cytochrome P-450 which were induced by acetone in chicken liver. All four forms of cytochrome P-450 proved to be distinct proteins, as indicated by their N-terminal amino acid sequences and their reconstituted catalytic activities. Two of these forms, also induced by glutethimide in chicken embryo liver, appeared to be cytochromes P450IIH1 and P450IIH2. Both of these cytochromes P-450 have identical catalytic activities towards benzphetamine demethylation. However, they differ in their abilities to hydroxylate p-nitrophenol and to convert acetaminophen into a metabolite that forms a covalent adduct with glutathione at the 3-position. Another form of cytochrome P-450 induced by acetone is highly active in the hydroxylation of p-nitrophenol and in the conversion of acetaminophen to a reactive metabolite, similar to reactions catalysed by mammalian cytochrome P450IIE. Yet the N-terminal amino acid sequence of this form has only 30-33% similarity with cytochrome P450IIE purified from rat, rabbit and human livers. A fourth form of cytochrome P-450 was identified whose N-terminal amino acid sequence and enzymic activities do not correspond to any mammalian cytochromes P-450 reported to be induced by acetone or ethanol.

scholarly journals Purification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus

1987 ◽  
Vol 15 (14) ◽  
pp. 5529-5544 ◽  
Author(s):  
William D. Henner ◽  
Natasha P. Kiker ◽  
Timothy J. Jorgensen ◽  
Jean-Nicholas Munck
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Calf Thymus ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The tertiary phase of rennin action on αs- and β-caseins

1970 ◽  
Vol 37 (3) ◽  
pp. 437-444 ◽  
Author(s):  
A. M. El-Negoumy
Keyword(s):  
Amino Acid ◽  
Degradation Product ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Starch Gel Electrophoresis ◽  
Terminal Amino Acid ◽  
Starch Gel ◽  
Terminal Amino

SummaryCasein, whole αs-casein and β-casein were incubated for 3 and 14 h with crystalline rennin, at pH 6·60 and 36 °C, both in phosphate buffer and in milk dialysate. Products obtained from both systems, comprising 30–83% calciumsensitive (Cas) components, gave similar patterns on starch gel electrophoresis. Whole casein and whole αs-casein were not so soluble in milk dialysate as in phosphate buffer. No significant differences in composition were observed between the Cas and the calcium-insensitive (Ca1) products from the same source.The αs1-component of the Cas product from rennin-treated whole αs-casein had faster gel mobility in comparison to the αs1-component in the Cas product from untreated whole αs-casein. Also, αs1-casein yielded one faster-moving degradation product, while αs2,3,4 appeared unaltered after 14h. The Cas product of rennintreated β-casein also had faster mobility than untreated β-casein and yielded one faster degradation product and several minor ones of slower mobility. Arginine was the only N-terminal amino acid found in the Cas product of both rennin-treated and untreated αs - and β-caseins. The arginine content increased from 3·48 and 4·98 moles/105g to 5·12 and 6·38 moles/105g in the Cas products from rennin-treated β-and αs-caseins, respectively.

Thermolytic digest of chicken pepsin

1981 ◽  
Vol 46 (8) ◽  
pp. 1994-2004 ◽  
Author(s):  
Miroslav Baudyš ◽  
Vladimír Kostka ◽  
Helena Keilová
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Linear Structure ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence ◽  
High Voltage Electrophoresis ◽  
Final Purification

Chicken pepsin prepared by the activation of pepsinogen was digested with thermolysin. The thermolytic digest was fractionated by chromatography on Sephadex G-25 fine. Certain fractions were subsequently subjected to ion exchange chromatography on Dowex 50-X2. The final purification was effected by paper chromatography and high voltage electrophoresis. By these procedures a series of homogeneous peptides was obtained; of the latter 54 nonoverlapping (save for a few exceptions) peptides are described in this paper. These peptides in addition to the thermolytic peptides reported before represent 80% of the linear structure of the whole molecule. The N-terminal amino acid sequence of chicken pepsin is discussed from the viewpoint of the recent data obtained by the analysis of the thermolytic digest.

scholarly journals Two globin strains in the giant annelid extracellular haemoglobins

1987 ◽  
Vol 241 (2) ◽  
pp. 441-445 ◽  
Author(s):  
T Gotoh ◽  
F Shishikura ◽  
J W Snow ◽  
K I Ereifej ◽  
S N Vinogradov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lumbricus Terrestris ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Reverse Phase ◽  
Terminal Amino ◽  
Polypeptide Chains

The constituent polypeptide chains I, II, III and IV of the giant extracellular haemoglobin of the oligochaete Lumbricus terrestris were isolated by mono Q ion-exchange chromatography and C8 reverse-phase chromatography. The N-terminal amino acid sequences of Lumbricus chains I, III and IV were determined and aligned with those of Lumbricus chain II and the four chains of the extracellular haemoglobin of the polychaete Tylorrhynchus heterochaetus. Three invariant amino acid residues, Cys-7, Val-15 and Trp-19, were found to occur in the N-terminal segments (17-22 residues) of the eight chains of Lumbricus and Tylorrhynchus haemoglobins. In addition, it was found that the eight sequences could be separated into two groups: ‘A’, consisting of Lumbricus chains I and II and Tylorrhynchus chains I and IIA, having invariant Lys-14 and Lys-16, and ‘B’, consisting of Lumbricus chains III and IV and Tylorrhynchus IIB and IIC, having invariant Cys-6, Ser-8 and Asp-11. This result suggests that there are two strains of globin chain in the annelid extracellular haemoglobins.

Fractionation of hordein by preparative, continuous carrier-free electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1301-1307 ◽  
Author(s):  
Ch. Ivanov ◽  
B. Mesrob ◽  
Z. Prusik
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Basic Fraction ◽  
Acidic Amino Acids ◽  
Carrier Free ◽  
Terminal Amino

Barley hordein was fractionated by preparative, continuous carrier-free electrophoresis. Six fractions were obtained, one of which was in negligible quantity. Three of the fractions gave single symmetrical peaks. The amino acid content and the N-terminal amino acid residues of these fractions were determined. The ratios of basic to acidic amino acids showed that the fractions contained different protein substances. The most basic fraction, representing 10% of the total hordein, appeared to be pure since it contained only alanine as a N-terminal amino acid.

The Enzymic Digestion of Cod Tropomyosin

1962 ◽  
Vol 19 (6) ◽  
pp. 1095-1104
Author(s):  
B. Truscott ◽  
P. L. Hoogland ◽  
P. H. Odense ◽  
A. E. Waddell
Keyword(s):  
Amino Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Enzymic Digestion ◽  
Disulphide Bonds ◽  
Terminal Amino

Tropomyosin from cod muscle can be oxidized with performic acid to cleave disulphide bonds without degradation of other amino acid residues. The ε-amino groups of lysine within the molecule can be substituted readily with carbobenzoxy-groups for protection against digestion by trypsin. The digestions by trypsin of carbobenzoxy-substituted tropomyosin, and by chymotrypsin of oxidized tropomyosin, have been shown to be reproducible, providing peptides suitable for amino acid sequence studies. The peptides so obtained were separated by ion-exchange chromatography using a Beckman/Spinco Amino Acid Analyzer.After treatment with urea, cod tropomyosin does not yield a free N-terminal amino acid as has been reported for rabbit tropomyosin.

scholarly journals Rapid purification and properties of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae

1978 ◽  
Vol 173 (3) ◽  
pp. 773-786 ◽  
Author(s):  
K A Bostian ◽  
G F Betts
Keyword(s):  
Amino Acid ◽  
Aldehyde Dehydrogenase ◽  
Amino Acid Content ◽  
Binding Studies ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Direct Binding ◽  
Terminal Amino ◽  
Rapid Purification

A method for the purification of yeast K+-activated aldehyde dehydrogenase is presented which can be completed in substantially less time than other published procedures. The enzyme has a different N-terminal amino acid from preparations previously reported, and other small differences in amino acid content. These differences may be the result of differential proteolytic digestion rather than a different protein in vivo. A purification step involves the biospecific adsorption on affinity columns containing immobilized nucleotides in the absence of the substrate aldehyde. Direct binding studies with the coenzyme in the absence of aldehyde reveal 4 NAD sites per tetrameric molecule, each with a dissociation constant of 120 micron. These results conflict with properties of preparations previously reported and may conflict with kinetic models that have aldehyde as the leading substrate. Binding to Blue Dextran affinity columns suggests the presence of a dinucleotide fold in common with other dehydrogenases and kinases.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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