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1.

Specificity of milk-clotting enzymes towards bovine kappa-casein.

Drøhse, H B; Foltmann, B.

Biochim Biophys Acta ; 995(3): 221-4, 1989 May 01.

Artículo en Inglés | MEDLINE | ID: mdl-2495817

2.

An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa.

Tarasova, N I; Szecsi, P B; Foltmann, B.

Biochim Biophys Acta ; 880(1): 96-100, 1986 Jan 15.

Artículo en Inglés | MEDLINE | ID: mdl-3510671

3.

Isolation and partial characterization of prochymosin and chymosin from cat.

Jensen, T; Axelsen, N H; Foltmann, B.

Biochim Biophys Acta ; 705(2): 249-56, 1982 Jul 26.

Artículo en Inglés | MEDLINE | ID: mdl-6810938

4.

Separation of porcine pepsinogen A and progastricsin. Sequencing of the first 73 amino acid residues in progastricsin.

Foltmann, B; Drøhse, H B; Nielsen, P K; James, M N.

Biochim Biophys Acta ; 1121(1-2): 75-82, 1992 May 22.

Artículo en Inglés | MEDLINE | ID: mdl-1599954

5.

The primary structure and enzymic properties of porcine prochymosin and chymosin.

Houen, G; Madsen, M T; Harlow, K W; Lønblad, P; Foltmann, B.

Int J Biochem Cell Biol ; 28(6): 667-75, 1996 Jun.

Artículo en Inglés | MEDLINE | ID: mdl-8673731

6.

Activation of human pepsinogens.

Foltmann, B.

FEBS Lett ; 241(1-2): 69-72, 1988 Dec 05.

Artículo en Inglés | MEDLINE | ID: mdl-3197840

7.

Seminal pepsinogen C is not identical with, but is very similar to gastric pepsinogen C.

Szecsi, P B; Koch, C; Foltmann, B.

FEBS Lett ; 238(1): 101-4, 1988 Sep 26.

Artículo en Inglés | MEDLINE | ID: mdl-3169243

8.

Determination of pepsin (EC 3.4.23.1) and gastricsin (EC 3.4.23.3) in gastric juice by rocket immunoelectrophoresis.

Axelsson, C K; Axelsen, N H; Szecsi, P B; Foltmann, B.

Clin Chim Acta ; 129(3): 323-31, 1983 Apr 25.

Artículo en Inglés | MEDLINE | ID: mdl-6406106

9.

Comparison of the primary structures of acidic proteinases and of their zymogens.

Foltmann, B; Pedersen, V B.

Adv Exp Med Biol ; 95: 3-22, 1977.

Artículo en Inglés | MEDLINE | ID: mdl-22997

10.

Chymosin: a short review on foetal and neonatal gastric proteases.

Foltmann, B.

Scand J Clin Lab Invest Suppl ; 210: 65-79, 1992.

Artículo en Inglés | MEDLINE | ID: mdl-1455182

11.

Gastric proteinases--structure, function, evolution and mechanism of action.

Foltmann, B.

Essays Biochem ; 17: 52-84, 1981.

Artículo en Inglés | MEDLINE | ID: mdl-6795036

12.

The N-terminal amino acid sequence of bovine pepsin (EC 3.4.4.1) and the sequence overlapping the activation fragment.

Harboe, M; Foltmann, B.

FEBS Lett ; 34(2): 311-4, 1973 Aug 15.

Artículo en Inglés | MEDLINE | ID: mdl-4583851

13.

Bovine pepsin: the sequence of the first 65 amino acid residues (completing the sequence of the first 110 residues of bovine pepsinogen).

Harboe, M K; Foltmann, B.

FEBS Lett ; 60(1): 133-6, 1975 Dec 01.

Artículo en Inglés | MEDLINE | ID: mdl-776669

14.

The amino acid sequence of the first 61 residues of chymosin (rennin EC 3.4.4.3).

Pedersen, V B; Foltmann, B.

FEBS Lett ; 35(2): 250-4, 1973 Sep 15.

Artículo en Inglés | MEDLINE | ID: mdl-4582940

15.

The amino acid sequence of a hitherto unobserved segment from porcine pepsinogen preceeding the N-terminus of pepsin.

Pedersen, V B; Foltmann, B.

FEBS Lett ; 35(2): 255-6, 1973 Sep 15.

Artículo en Inglés | MEDLINE | ID: mdl-4582941

16.

Identification of an enzymatically active intermediate in the activation of porcine pepsinogen.

Christensen, K A; Pedersen, V B; Foltmann, B.

FEBS Lett ; 76(2): 214-8, 1977 Apr 15.

Artículo en Inglés | MEDLINE | ID: mdl-16778

17.

Comparative investigations on pig gastric proteases and their zymogens.

Foltmann, B; Harlow, K; Houen, G; Nielsen, P K; Sangild, P.

Adv Exp Med Biol ; 362: 41-51, 1995.

Artículo en Inglés | MEDLINE | ID: mdl-8540351

18.

Structure and function of proparts in zymogens for aspartic proteinases.

Foltmann, B.

Biol Chem Hoppe Seyler ; 369 Suppl: 311-4, 1988 May.

Artículo en Inglés | MEDLINE | ID: mdl-3060143

19.

Activation of porcine pepsinogen A. The stability of two non-covalent activation intermediates at pH 8.5.

Nielsen, F S; Foltmann, B.

Eur J Biochem ; 217(1): 137-42, 1993 Oct 01.

Artículo en Inglés | MEDLINE | ID: mdl-8223551

20.

Purification and characterization of porcine pepsinogen B and pepsin B.

Nielsen, P K; Foltmann, B.

Arch Biochem Biophys ; 322(2): 417-22, 1995 Oct 01.

Artículo en Inglés | MEDLINE | ID: mdl-7574716

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Specificity of milk-clotting enzymes towards bovine kappa-casein.

An aspartic proteinase from human erythrocytes is immunochemically indistinguishable from a non-pepsin, electrophoretically slow moving proteinase from gastric mucosa.

Isolation and partial characterization of prochymosin and chymosin from cat.

Separation of porcine pepsinogen A and progastricsin. Sequencing of the first 73 amino acid residues in progastricsin.

The primary structure and enzymic properties of porcine prochymosin and chymosin.

Activation of human pepsinogens.

Seminal pepsinogen C is not identical with, but is very similar to gastric pepsinogen C.

Determination of pepsin (EC 3.4.23.1) and gastricsin (EC 3.4.23.3) in gastric juice by rocket immunoelectrophoresis.

Comparison of the primary structures of acidic proteinases and of their zymogens.

Chymosin: a short review on foetal and neonatal gastric proteases.

Gastric proteinases--structure, function, evolution and mechanism of action.

The N-terminal amino acid sequence of bovine pepsin (EC 3.4.4.1) and the sequence overlapping the activation fragment.

Bovine pepsin: the sequence of the first 65 amino acid residues (completing the sequence of the first 110 residues of bovine pepsinogen).

The amino acid sequence of the first 61 residues of chymosin (rennin EC 3.4.4.3).

The amino acid sequence of a hitherto unobserved segment from porcine pepsinogen preceeding the N-terminus of pepsin.

Identification of an enzymatically active intermediate in the activation of porcine pepsinogen.

Comparative investigations on pig gastric proteases and their zymogens.

Structure and function of proparts in zymogens for aspartic proteinases.

Activation of porcine pepsinogen A. The stability of two non-covalent activation intermediates at pH 8.5.

Purification and characterization of porcine pepsinogen B and pepsin B.