3.4.23.1

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Peptic peptides from the beta polypeptide chain of AII component of chicken hemoglobin.

T Maita et al.

Journal of biochemistry, 78(6), 1311-1319 (1975-12-01)

The aminoethylated beta polypeptide chain of AII component from chicken hemoglobin was digested with pepsin [EC 3.4.23.1] and the resulting peptides were separated and purified by gel filtration, ion exchange chromatography, and paper chromatography. The amino acid composition and partial

Cleavage of human serum immunoglobulin G by an immobilized pepsin preparation.

T Tomono et al.

Biochimica et biophysica acta, 660(2), 186-192 (1981-08-13)

In order to obtain an efficacious and safe immunoglobulin G (IgG) preparation for intravenous use, the digestion of IgG with an immobilized pepsin (EC 3.4.23.1) preparation was studied. Thus, pepsin was immobilized onto glutaraldehyde-activated AH-Sepharose 4B under acidic conditions. THe

The primary structure of calf chymosin.

B Foltmann et al.

The Journal of biological chemistry, 254(17), 8447-8456 (1979-09-10)

The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously

An in vitro procedure for studying enzymic dephosphorylation of phytate in maize-soyabean feeds for turkey poults.

K Zyła et al.

The British journal of nutrition, 74(1), 3-17 (1995-07-01)

An in vitro method was developed to predict inorganic P release from maize-soyabean poultry feeds containing supplemental phytase (EC 3.1.3.8), and to quantify the effect of acid phosphatase (EC 3.1.3.2), fungal protease (EC 3.4.23.6) and Aspergillus niger cellulase (EC 3.2.1.4)

The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus.

W J Chang et al.

Journal of biochemistry, 80(5), 975-981 (1976-11-01)

1. The Type B acid protease from Aspergillus niger var. macrosporus was inactivated by reaction with diazoacetyl-DL-norleucine methyl ester (DAN), DL-1-diazo-3-tosylamido-2-heptanone (DTH), and L-1-diazo-3-tosylamido-4-phenyl-2-butanone (DTPB) in the presence of cupric ions. The reaction with DAN took place with 1:1 stoichiometry.

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