Amino acid sequence of cyanogen bromide fragments CB4 and CB6 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 626-639
Author(s):  
Ladislav Morávek

By the analyses of chymotryptic, and thermolytic peptides the amino acid sequence was determined of cyanogen bromide fragment CB4 representing the region of the pepsin chain between the N-terminus and methonine-residue I: Ile-Gly-Asp-Glu-Pro-Leu-Glu-Asn-Tyr-Leu-Asp-Thr-Glu-Tyr-Phe-Gly-Thr-Ile-Gly-Ile-Gly-Thr-Pro-Ala-Gln-Asp-Phe-Thr-Val-Ile-Phe-Asp-Thr-Gly-Ser-Ser-Asn-Leu-Trp-Val-Pro-Ser-Val-Tyr-Cys-Ser-Ser-Leu-Ala-Cys-Ser-Asp-His-Asn- + Gln-Phe-Asn-Pro-Asp-Asp-Ser-Ser-Thr-Phe-Glu-Ala-Thr-Ser-Gln-Glu-Leu-Ser-Ile-Thr-Tyr-Gly- + Thr-Gly-Ser-Met. The serine residue (Ser) in position 68 of pepsin is phosphorylated. By sequential analysis of chymotryptic, tryptic, and thermolytic peptides the amino acid sequence was determined of cyanogen bromide fragment CB6 representing the region between methionine residues II and III in the pepsin chain: Asp-Gly-Glu-Thr-Ile-Ala-Cys-Ser-Gly-Gly-Cys-Gln-Ala- + Ile-Val-Asp-Thr-Gly-Thr-Ser-Leu-Leu-Thr-Gly-Pro-Thr-Ser-Ala-Ile-Ala-Asn-Ile-Gln-Ser-Asp- + Ile-Gly-Ala-Ser-Glu-Asn-Ser-Asp-Gly-Glu-Met. The aspartic acid residue (Asp) in position 16 of this fragment is identical with the residue reacting with diazo inhibitors which forms a part of the active center of the enzyme. Both half-cystine residues of fragment CB4 and fragment CB6 are linked to one another by a disulfide bond in native pepsin.

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.


1977 ◽  
Vol 30 (2) ◽  
pp. 1 ◽  
Author(s):  
MichaeI Coates ◽  
B Brimhall ◽  
Peter Stenzel ◽  
Mark Hermodson ◽  
David Gibson ◽  
...  

The amino acid sequence of the IX-chain of the major haemoglobin of a newt, T. granulosa, has been determined. The chain is 142 residues long and has an extra methionine at its N-terminus when compared with human IX-chain. Most of the tryptic peptides were sequenced by a combination of the subtractive Edman method and by deduction from the compositions of overlapping fragments produced by various enzymic treatments. The sequence of two 'core' regions was obtained by automatic sequencing of large peptides produced by trypsin cleavage at arginine residues only after blockage of lysine residues by citraconylation; by cleavage between aspartic acid and proline residues with 70% formic acid, and by cyanogen bromide cleavage at methionine residues.


1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.


1976 ◽  
Vol 7 (10) ◽  
pp. no-no
Author(s):  
L. MORAVEK ◽  
V. KOSTKA ◽  
I. ROSENBERG ◽  
B. MELOUN ◽  
M. A. SABER

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