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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] and the resulting peptides were separated and purified by gel filtration, ion exchange chromatography, and paper chromatography. The amino acid composition and partial
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 preparation was studied. Thus, pepsin was immobilized onto glutaraldehyde-activated AH-Sepharose 4B under acidic conditions. THe
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 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
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, and to quantify the effect of acid phosphatase (EC, fungal protease (EC and Aspergillus niger cellulase (EC
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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