The Primary Structure Of Crotalase, A Thrombin-Like Venom Enzyme, Exhibits Strong Homology With Kallikrein

1981 ◽  
Author(s):  
H Pirkle ◽  
F S Markland ◽  
S S Bajwa ◽  
I Theodor ◽  
R Baumgartner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Edman Degradation ◽  
Terminal Amino Acid ◽  
Internal Sequence ◽  
Strong Homology ◽  
Terminal Amino ◽  
Homologous Alignment ◽  
Terminal Amino Acid Sequence

Edman degradation of crotalase and its tryptic and CNBr fragments yielded an N-terminal amino acid sequence, Val- Ile-Gly-Gly-Asp-Glu-Cys-AsN-Ile-AsN-Glu-His-Arg-Phe-Leu-Val- Ala-Leu-Tyr-Asp-Tyr-Trp-Xxx-GlN-Xxx-Phe-rLeu-, and internal sequences, -Leu-Ile-Arg-Leu-AsN-Lys-Pro-Val-Ser-Tyr-Ser-Glu- His-Ile-Ala-Pro-Leu-Ser-Leu-Pro-Ser-Ser-Pro-Pro-Ile-Val-Gly- Ser-Val-Cys-Arg-Ala-Met-Gly-Trp-Gly-GIN-Thr-Thr-Ser-Pro-GIN- Glu-Thr-Leu-Pro-Asp-Val-Pro-His-Cys-Ala-AsN-Ile-AsN-Leu-Leu- Asp-Tyr-Glu-Val-Cys- and -Ser-Val-GIN-Phe-Asp-Lys-Glu-GIN- GIN-Arg-. The longer internal sequence aligns homologously with positions 105-168 of chymotrypsinogen with gaps, each 5 residues long, following Pro 128 and GIN 143. No homologous alignment has been found for the shorter internal sequence. These findings led to experiments which demonstrated that crotalase has specific enzymatic properties resembling kallikrein.

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.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

Sign in / Sign up

Export Citation Format

Share Document