scholarly journals Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2

1975 ◽  
Vol 145 (3) ◽  
pp. 459-467 ◽  
Author(s):  
D Parris ◽  
L S Swart
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Paper Chromatography ◽  
Deae Cellulose ◽  
Edman Degradation ◽  
Sequence Determination ◽  
Terminal Amino Acid ◽  
Partial Acid Hydrolysis ◽  
Terminal Amino

The complete amino acid sequence of mohair protein, SCMKB-M1.2 (97 residues), was determined. The protein was isolated from reduced and carboxymethylated mohair by chromatography on DEAE-cellulose phosphate. Peptides for sequence determination were obtained by digestion with trypsin, pepsin, chymotrypsin, thermolysin and papain, and were fractionated by DEAE-cellulose chromatography, paper chromatography and electrophoresis. The sequence of the peptides were determined by the Edman degradation method (by use of both the Beckman Sequence and a non-automatic procedure), and by partial acid hydrolysis. The protein is closely homologous to wool protein SCMKB-IIIB2, and also contains acetylated alanine as N-terminal amino acid.

The N-terminal Amino Acid Sequence of Sheep Heart Myoglobin

1972 ◽  
Vol 27 (2) ◽  
pp. 157-159 ◽  
Author(s):  
Walter Vötsch ◽  
F. Alfred Anderer
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Layer Chromatography ◽  
Terminal Amino Acid Sequence

The N-terminal amino acid sequence of residues 1—50 of sheep heart myoglobin was determined using the automatic Edman degradation procedure. The amino acid phenyl-thiohydantoins were identified by thin layer chromatography and/or by mass spectrometry.

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).

Sign in / Sign up

Export Citation Format

Share Document