about
The amino acid sequence of dromedary pancreatic ribonucleaseIn vitro protein synthesis: chain initiation.Isolation and characterization of a 60-residue intestinal peptide structurally related to the pancreatic secretory type of trypsin inhibitor: influence on insulin secretionThe mechanism of pepsin action.Isolation and characterization of porcine diazepam-binding inhibitor, a polypeptide not only of cerebral occurrence but also common in intestinal tissues and with effects on regulation of insulin release.The amino acid sequences of cytochromes c-551 from three species of PseudomonasIsolation and point of action of a factor from Escherichia coli required to reconstruct translation.Chymotrypsincatalysed transpeptidations.Peptide bond formation stimulated by protein synthesis factor EF-P depends on the aminoacyl moiety of the acceptor.Hydrolysis and transpeptidation of lysine peptides by trypsin.The active centre of triose phosphate isomerase.Acidic peptides of the lens. 4. The biosynthesis of ophthalmic acid.Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.[Nucleophilic competition in enzymic hydrolytic reactions. Kinetic analysis and application to the tryptic hydrolysis of some esters].Metabolism of aromatic compounds by fungi. 2. Subunit structure of the 3-carboxy-cis-cis-muconate cyclase of Aspergillus niger.Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II.Thioredoxin. 5. Amino acid sequences of the tryptic peptides of peptide A.Thioredoxin. 3. Amino acid sequences of the peptic peptides from S-aminoethylated peptide B.[In vitro digestion apparatus for the enzymatic hydrolysis of proteins].Hæmoglobin–LeporeHollandia
P2860
Q30752822-5C3833B7-67EF-4795-B7BF-F526E0BC2FDBQ33802536-E1150F75-EB88-446C-A0DC-C18AFA03358BQ34317647-BB0C4027-7D36-4E19-85CF-6EF4D292EFE3Q36404135-2A2CFACA-8964-43E6-9EBC-434D259EB80EQ36445712-ADAFDAD2-19E7-4165-99D5-60108DD349E6Q36512807-0900122B-5B15-49F8-AAB0-915E8EBE06C7Q37680344-271F518A-2A3D-4D24-B11D-4304A7010EF6Q39245036-79537168-7DE1-4520-B07D-1E92B69F2EE7Q41095698-14034A90-2B01-441C-A6A7-9DB8DE1AA650Q41942104-12045AD5-579B-4465-AB84-AFFBCD5DD6F2Q42094648-BEDF5785-7F72-42BC-91BF-3B032FD6CC0AQ42223188-54F05FA9-F4F8-4767-9BF7-79DE199224DEQ42853145-34179644-D955-426A-B659-C6BF1739C152Q44114801-57536D6D-C0A6-47D5-A0A4-22621FBAF7E2Q46819532-131E1173-0964-4C41-8BB5-5A5254B7201EQ47731833-78FE5F23-9624-4C93-BCE0-962FBA8EBABBQ47802986-B5C993E5-45A2-4F7A-B0B6-7B1B7C6E5A62Q47807260-A8852121-8792-4043-9362-462E1CB220E6Q53752605-11A37417-18FC-4393-AC98-ED7D8CCF88F1Q59002649-B84743E5-5E04-48C1-8AE6-CE8F5B4C1AB5
P2860
description
1954 nî lūn-bûn
@nan
1954年の論文
@ja
1954年学术文章
@wuu
1954年学术文章
@zh-cn
1954年学术文章
@zh-hans
1954年学术文章
@zh-my
1954年学术文章
@zh-sg
1954年學術文章
@yue
1954年學術文章
@zh
1954年學術文章
@zh-hant
name
Trypsin-catalysed transpeptidations.
@en
Trypsin-catalysed transpeptidations.
@nl
type
label
Trypsin-catalysed transpeptidations.
@en
Trypsin-catalysed transpeptidations.
@nl
prefLabel
Trypsin-catalysed transpeptidations.
@en
Trypsin-catalysed transpeptidations.
@nl
P2860
P356
P1433
P1476
Trypsin-catalysed transpeptidations.
@en
P2093
P2860
P304
P356
10.1042/BJ0570529
P407
P577
1954-08-01T00:00:00Z