scholarly journals The complete amino acid sequence of a mouse ϰ light chain

1972 ◽  
Vol 128 (2) ◽  
pp. 427-444 ◽  
Author(s):  
J. Svasti ◽  
C. Milstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Paper Electrophoresis ◽  
Tryptic Peptides ◽  
Myeloma Protein ◽  
Complete Amino Acid Sequence ◽  
Cellulose Column ◽  
Mouse Myeloma

The complete amino acid sequence of the κ-chain of the mouse myeloma protein MOPC 21 was established. The protein was reduced and alkylated with iodo[2-14C]acetic acid, and 21 tryptic peptides were isolated, mainly by paper electrophoresis and paper chromatography. Three large tryptic peptides (of 35, 36 and 42 residues), which were difficult to isolate in this manner, were obtained pure and in excellent yields by a combination of Sephadex G-50 gel filtration in 1% (w/v) NH4HCO3 and chromatography on a DEAE-cellulose column in ammonium acetate buffer, pH8.1. Peptides overlapping the tryptic peptides were isolated from a chymotryptic digest. The chain is 214 residues long. Microheterogeneity of two peptides was observed and is believed to be due to deamidation. It was not excluded that such deamidation could occur in serum from which the protein was isolated. The sequence is compared with the sequences of two other mouse κ-chains, and with the human κ-chain basic sequences.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

The Complete Amino-Acid Sequence of the Heavy Chain of the Human Myeloma Protein WIE, an Immunoglobulin D

1991 ◽  
Vol 372 (2) ◽  
pp. 795-818 ◽  
Author(s):  
R. Joachim FRIEDRICH ◽  
Rolf BÄTGE ◽  
Iris SCHRANNER ◽  
Ulrike KOTUCHA ◽  
Klaus ECKART ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Myeloma Protein ◽  
Complete Amino Acid Sequence ◽  
Immunoglobulin D

scholarly journals Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequence

1982 ◽  
Vol 207 (2) ◽  
pp. 253-260 ◽  
Author(s):  
M A Smith ◽  
L M Gerrie ◽  
B Dunbar ◽  
J E Fothergill
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Gel Filtration ◽  
Complete Amino Acid Sequence ◽  
The Third ◽  
Human Sequence ◽  
Bovine Plasma ◽  
Bovine Sequence ◽  
C 50

Purification of C4a from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a has been determined by automatic sequencer degradation of CNBr and enzymic fragments, and by carboxypeptidase digestion. The 77-residue bovine sequence shows 12 differences from the human sequence with five of these differences occurring in the C-terminal 11 residues. The sequence of C4a confirms earlier suggestions of homology with C3a and C5a: the three sequences show an almost equal number of identities with each other. The six cysteine residues of the ‘disulphide knot’ are conserved as well as seven other residues including the C-terminal arginine.

scholarly journals Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-IIIA3

1973 ◽  
Vol 133 (4) ◽  
pp. 641-654 ◽  
Author(s):  
Louis S. Swart ◽  
Thomas Haylett
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Minor Component ◽  
Amino Acid Sequences ◽  
Edman Degradation ◽  
Merino Wool ◽  
C Terminus ◽  
A Minor

The complete amino acid sequences of wool protein SCMKB-IIIA3 (131 residues) and a minor component SCMKB-IIIA3A (130 residues) have been determined. The proteins are mutually homologous and have free threonine as the N-terminal residue and carboxymethylcysteine as the C-terminus. The peptides used for the sequence work were obtained by trypsin, thermolysin, pepsin and chymotrypsin digestions and were fractionated by chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 and G-50, paper chromatography and electrophoresis. The Edman degradation method (employing both the Beckman Sequencer and a non-automatic procedure) was used to obtain the sequences of the peptides.

Amino Acid Sequence Studies of Horseradish Peroxidase. I. Tryptic Peptides

1972 ◽  
Vol 50 (1) ◽  
pp. 44-62 ◽  
Author(s):  
K. G. Welinder ◽  
L. B. Smillie ◽  
G. R. Schonbaum
Keyword(s):  
Amino Acid ◽  
Horseradish Peroxidase ◽  
Amino Acid Sequence ◽  
Paper Electrophoresis ◽  
Iodoacetic Acid ◽  
Performic Acid ◽  
Cysteic Acid ◽  
Acid Oxidation ◽  
Tryptic Peptides ◽  
Tryptic Digest

Commercially available horseradish peroxidase (RZ 3.1) was characterized with respect to its homogeneity by (1) chromatography on CM-cellulose, (2) disc gel electrophoresis in alkaline and acidic buffers, (3) micro-scale sucrose gradient isoelectrofocusing in pH 3–10 and pH 8–10 gradients, (4) gel isoelectrofocusing in pH 3–10 and pH 8–10 gradients, and (5) amino acid and hexosamine analyses. The preparation was found to be highly homogeneous except by pH 8–10 gel isoelectrofocusing which resolved it into several very close bands. This heterogeneity has been assumed to reflect differences in carbohydrate composition rather than in the amino acid sequence or composition. Amino acid analyses after performic acid oxidation yielded eight cysteic acid residues per mole of enzyme. Since no S-carboxymethylcysteine was recovered after treatment of the protein in 8 M urea with iodoacetic acid, it was concluded that the enzyme has four disulfide bridges. Peptides resulting from a tryptic digest of the heme-free enzyme were purified by high-voltage paper electrophoresis and subjected to sequence analysis. Several half-cystine sequences were elucidated after isolation of the radioactive peptides from a tryptic digest of the reduced and 14C-S-carboxymethylated protein. The complete sequences of 21 and partial sequences of three tryptic peptides were determined. These account for 203 of the approximately 300 amino acid residues of this protein. Several sites of carbohydrate attachment were observed.

scholarly journals Amino Acid Sequence of the Light Chain from a Mouse Myeloma Protein with Anti-Hapten Activity: Evidence for a Third Type of Light Chain

1971 ◽  
Vol 68 (11) ◽  
pp. 2623-2626 ◽  
Author(s):  
E. P. Schulenburg ◽  
E. S. Simms ◽  
R. G. Lynch ◽  
R. A. Bradshaw ◽  
H. N. Eisen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Myeloma Protein ◽  
Mouse Myeloma

Human hemopexin. Preparation of the heme-rich protein

1982 ◽  
Vol 47 (2) ◽  
pp. 535-542 ◽  
Author(s):  
Ladislav Morávek ◽  
Josef Borvák ◽  
Karel Grüner ◽  
Bedřich Meloun ◽  
Petr Štrop ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Analysis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Simplified Procedure ◽  
Pooled Samples ◽  
Terminal Amino Acid Sequence

A simplified procedure was developed for the preparation of hemopexin from Cohn fraction IV obtained from partially hemolyzed pooled samples of serum. The method is based on precipitation with rivanol, chromatography on DEAE-cellulose, and gel filtration; it permits large quantities of the material to be treated on a laboratory scale. The preparation of heme-rich hemopexin obtained was characterized by amino acid analysis and the following N-terminal amino acid sequence: Thr-Pro-Leu-Pro-Arg-Gly-Ser-Ala-His-Gly-Asn-Val-Ala-Glu-Gly-Glu-Thr(Thr)Thr-Asn-Pro-Asp-Val-(Gly)(Leu).

scholarly journals Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides

1983 ◽  
Vol 213 (1) ◽  
pp. 31-38 ◽  
Author(s):  
N Tamiya ◽  
N Maeda ◽  
H G Cogger
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
British Library ◽  
Amino Acid Residues ◽  
Protein Amino Acid ◽  
Tryptic Peptides ◽  
Sea Snakes ◽  
And Migration

The main neurotoxic components, toxins Hydrophis ornatus a and Hydrophis lapemoides a, were isolated from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides respectively. The amino acid sequence of toxin Hydrophis ornatus a was deduced to be identical with that of toxin Astrotia stokesii a [Maeda & Tamiya (1978) Biochem. J. 175, 507-517] on the basis of identity of the tryptic peptide ‘map’ and the amino acid composition of each peptide. The amino acid sequence of toxin Hydrophis lapemoides a was determined mainly on the basis of identity of the amino acid compositions, mobilities on paper electrophoresis and migration positions on paper chromatography of the tryptic peptides with those of other sea-snake toxins whose sequences are known. Both toxins Hydrophis ornatus a and Hydrophis lapemoides a consisted of 60 amino acid residues and there were six amino acid replacements between them. The taxonomy of sea snakes in the Hydrophis ornatus complex has long been confused, and the above snakes were originally assigned to taxa that proved to be inconsistent with the relationships indicated by the neurotoxin amino acid sequences obtained. A subsequent re-examination of the specimens revealed an error in the original identifications and demonstrated the value of the protein amino acid sequences in systematic and phylogenetic studies. The isolation procedure and results of amino acid analysis of the tryptic peptides have been deposited as Supplementary Publication SUP 50121 (8 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1983) 209, 5.

Sign in / Sign up

Export Citation Format

Share Document