scholarly journals Myoglobins of Cartilaginous Fishes III. Amino Acid Sequence of Myoglobin of the Shark Galeorhinus Australis

1981 ◽  
Vol 34 (1) ◽  
pp. 5 ◽  
Author(s):  
WK Fisher ◽  
DD Koureas ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Red Muscle ◽  
Cartilaginous Fishes ◽  
Port Jackson

Myoglobin isolated from the red muscle of the school shark Galeorhinus australis was purified by gel filtration and ion-exchange chromatography. The amino acid sequence was determined following digestion with trypsin and purification of the peptides by paper ionophoresis and chromatography. Sequences of purified peptides were determined by the dansyl-Edman procedure and the peptides aligned by homology with the sequence of the myoglobin of the gummy shark Mustelus antarcticus. The two myoglobin sequences showed a marked similarity (16 differences), but both sequences showed approximately the same number of differences (68) from myoglobin of the Port Jackson shark Heterodontus portusjacksoni. There are 19 residues unique to the three shark myoglobin sequences.

scholarly journals Studies on Marsupial Protein. II. Amino Acid Sequence of the -Chain of Haemoglobin from the Grey Kangaroo, Macropus Giganteus

1969 ◽  
Vol 22 (6) ◽  
pp. 1437 ◽  
Author(s):  
GM Air ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Grey Kangaroo

The amino acid sequence of the jS-chain of haemoglobin from M. giganteus has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, ion-exchange chromatography, and paper ionophoresis, and amino acid sequences determined by the "dansyl"-Edman procedure. Special procedures were necessary for three peptides which were insoluble.

scholarly journals Myoglobins of Cartilaginous Fishes. II. Isolation and Amino Acid Sequence of Myoglobin of the Shark Mustelus Antarcticus

1980 ◽  
Vol 33 (2) ◽  
pp. 153 ◽  
Author(s):  
WK Fisher ◽  
DD Koureas ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Spectrographic Analysis ◽  
Amino Acid Residues ◽  
Sequence Determination ◽  
Amino Terminal ◽  
Red Muscle ◽  
Cartilaginous Fishes

Myoglobin isolated from red muscle of the gummy shark M. antarcticus was purified by gel filtration and ion-exchange chromatography on carboxymethyl cellulose in 8 M urea-thiol buffer. Amino acid analysis and sequence determination showed 148 amino acid residues. The amino terminal residue is acetylated as shown by nuclear magnetic resonance and mass spectrographic analysis of an N-terminal peptide. There is a deletion of four residues at the amino terminal end as well as one residue in the CD interhelical area relative to other myoglobins. These overall differences were also found previously in myoglobin of Heterodontus portusjacksoni.

Myoglobin of the Shark Heterodontus Portusjacksoni: Isolation and Amino Acid Sequence

1979 ◽  
Vol 32 (3) ◽  
pp. 277 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Spectrographic Analysis ◽  
Amino Acid Residues ◽  
Sequence Determination ◽  
Amino Terminal ◽  
Red Muscle

Myoglobin isolated from red muscle of the shark H. portusjacksoni was purified by ion-exchange chromatography on sulfopropyl-Sephadex and gel-filtration. Amino acid analysis and sequence determination showed 148 amino acid residues. The amino terminal residue is acetylated as shown by mass spectrographic analysis of N-terminal peptides. There is a deletion of four residues at the amino terminal end as well as one residue in the CD interhelical area relative to other myoglobins.

scholarly journals Isolation and a partial amino acid sequence of insulin from the islet tissue of cod (Gadus callarias)

1968 ◽  
Vol 106 (2) ◽  
pp. 531-541 ◽  
Author(s):  
P T Grant ◽  
K. B. M. Reid
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Bovine Insulin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Islet Tissue ◽  
A Chain

1. Insulin has been isolated by gel filtration and ion-exchange chromatography from extracts of the discrete islet tissue of cod. The final preparation yielded a single band on electrophoresis at two pH values. The biological potency was 11·5 international units/mg. in mouse-convulsion and other assay procedures. 2. Glycine and methionine were shown to be the N-terminal amino acids of the A and B chains respectively. An estimate of the molecular weight together with amino acid analyses indicated that cod insulin, like the bovine hormone, consists of 51 amino acid residues. In contrast, the amino acid composition differs markedly from bovine insulin. 3. Oxidation of insulin with performic acid yielded the A and B peptide chains, which were separated by ion-exchange chromatography. Sequence studies on smaller peptides isolated from enzymic digests or from dilute acetic acid hydrolysates of the two chains have established the sequential order of 14 of the 21 amino acid residues of the A chain and 25 of the 30 amino acid residues of the B chain.

scholarly journals Confirmation of the 1–20 amino acid sequence of human adrenocorticotrophin

1973 ◽  
Vol 133 (1) ◽  
pp. 11-13 ◽  
Author(s):  
H. P. J. Bennett ◽  
P. J. Lowry ◽  
C. McMartin
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Countercurrent Distribution ◽  
Edman Degradation ◽  
Sequence Determination ◽  
Carboxypeptidase B ◽  
Aminopeptidase M

The tryptic fragments of natural human adrenocorticotrophin, were separated by countercurrent distribution and a correction in positions 25, 26, 27 and 30 was made by Riniker et al. (1972) in a study of the fragment containing residues 22–39. We have purified the remaining tryptic fragments, namely residues 1–8, 9–15, 16–21 and 17–21, by using ion-exchange chromatography on CM-cellulose and have carried out sequence determination by using the subtractive Edman degradation procedure and digestion with aminopeptidase M and carboxypeptidase B. These results have confirmed the proposed sequence for human adrenocorticotrophin in regions 6–7, 10–14 and 17–20, which had previously been arrived at only by analogy with the invariant sequence found in the three other mammalian adrenocorticotrophin species that had been investigated.

Cyanogen Bromide Fragments of Rabbit Skeletal Tropomyosin

1973 ◽  
Vol 51 (1) ◽  
pp. 56-70 ◽  
Author(s):  
R. S. Hodges ◽  
L. B. Smillie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Coiled Coil ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Coil Structure ◽  
Polypeptide Chains

Previous studies have demonstrated that rabbit skeletal tropomyosin consists of two or more chemically non-identical but highly homologous polypeptide chains. Attempts by a variety of techniques to prepare pure tropomyosin chains in amounts adequate for chemical characterization have been unsuccessful to date. To provide more extensive information for the purpose of elucidating the relationship between amino acid sequence and the coiled-coil structure of tropomyosin, a cyanogen bromide treatment of the S-carboxymethylated protein was carried out. The fragments were separated into small and large components by gel filtration on Sephadex G-50. The small fragments were fractionated by ion-exchange chromatography and electrophoresis on paper and their sequences elucidated by conventional methods. Coupled with previous data, these results indicate a minimum of seven unique methionine sequences and are consistent with a high degree of homology in the tropomyosin polypeptide chains. From the mixture of the larger cyanogen bromide polypeptides, a fragment was isolated by ion-exchange chromatography on QAE-Sephadex. In aqueous buffer it had a molecular weight of 35 000 and an α-helical content of about 60% as estimated by circular dichroism. In 8 M urea its molecular weight was reduced to 15 000, a value in reasonable agreement with a minimal molecular weight of 17 000 calculated from its amino acid composition. From its histidine content (two residues) and the known COOH-terminal amino acid sequence of the protein, the fragment was concluded to be derived from the COOH-terminal half of the molecule. These results are consistent with a degree of 'coiled-coil' structure in a fragment representing about one-half of the tropomyosin molecule.

A NEUROPHYSIN FROM COD (GADUS MORRHUA) PITUITARY GLANDS: ISOLATION AND PROPERTIES

1968 ◽  
Vol 42 (1) ◽  
pp. 143-NP ◽  
Author(s):  
B. T. PICKERING
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Arginine Vasopressin ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Maximum Binding Capacity ◽  
Pituitary Glands

SUMMARY A protein capable of binding neurohypophysial hormones has been isolated from cod pituitary glands using gel filtration and ion-exchange chromatography. The cod protein which was acidic and rich in cystine had an amino acid composition closely related to those of the mammalian neurophysins. It had a maximum binding capacity of 2·2 μmole/14mg. for oxytocin, 2·1 μmole/14 mg. for [8-arginine]-oxytocin and 1·1 μmole/14 mg. for [8-arginine]-vasopressin. Thus the cod protein had a greater capacity for the endogenous pressor-antidiuretic peptide than for the analogous mammalian hormone.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Evaluation of dialysis treatment in uremic patients by gel filtration of serum

1990 ◽  
Vol 36 (11) ◽  
pp. 1906-1910 ◽  
Author(s):  
J Osada ◽  
T Gea ◽  
C Sanz ◽  
I Millan ◽  
J Botella
Keyword(s):  
Ion Exchange ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
The Other ◽  
Control Group ◽  
Dialysis Treatment ◽  
Additional Information ◽  
Molecular Masses ◽  
Two Peaks

Abstract A group of substances of molecular masses between 300 and 1500 Da have been found to be toxic metabolites in patients with uremia. We determined the concentration in serum of these molecules in the following groups of patients: two hemodialyzed groups (one with cuprophane and the other with polyacrylonitrile dialyzers), one group treated with continuous ambulatory peritoneal dialysis, one group of nondialyzed azotemic patients, and one control group of healthy persons. Ultrafiltrates of the subjects' sera were fractionated on Sephadex G-15 followed by ion-exchange chromatography. Eluates were monitored by absorbance at 254 and 206 nm. Partially characterized peaks P1 and P2, obtained by gel filtration, correlated with the concentration of creatinine in serum; their concentrations were significantly (P less than 0.01) larger in hemodialyzed groups than in peritoneal dialyzed or in nondialyzed azotemic patients. After ion-exchange chromatography, two peaks (P'5 and P'6) correlated with serum creatinine and also were larger in hemodialyzed patients than in the other groups. Apparently, adequate discrimination is obtained by gel-filtration analysis and further analysis by ion-exchange chromatography does not provide additional information in most of the affected patients.

scholarly journals Isolation, partial purification and characterization of phospholipase A2 from Naja Katiensis venom

2021 ◽  
Vol 13 (2) ◽  
pp. 107-112
Author(s):  
C.F. Okechukwu ◽  
P.L. Shamsudeen ◽  
R.K. Bala ◽  
B.G. Kurfi ◽  
A.M. Abdulazeez
Keyword(s):  
Ion Exchange ◽  
Phospholipase A2 ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Crude Venom

The most effective and acceptable therapy for snakebite victims is the immediate administration of antivenin which is limited by problems of hypersensitivity reactions in some individuals and its inability to resolve the local effects of the venom. The aim of this study was to isolate, partially purify and characterize phospholipase A2 from Naja Katiensis venom. Phospholipase A2 was partially purified via a two-step process: gel filtration on Sephadex G-75 and ion exchange chromatography using CM Sephadex, and subjected to SDS-PAGE analysis. From the results, the specific activity of the partially purified PLA2 decreased from 0.67μmol/min/mg in crude venom to 0.29μmol/min/mg after ion exchange chromatography with a yield of 5% and purification fold of 0.43. The optimum temperature of the purified PLA2 was found to be 35ºC and optimum p.H of 7. velocity studies for the determination of kinetic constants using L-a-lecithin as substrate revealed a Km  of 1.47mg/ml and Vmax  of 3.32μ moles/min/mg. The sodium dodecyl sulphate polyacrylamide gel electrophoresis of the purified PLA2 showed a distinct band with molecular weight estimated to be 14KDa. In conclusion, the present study shows that phospholipase A2 was isolated, purified and characterized. This may serve as a promising candidate for future development of a novel anti-venin drug.

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