Enzymatically active, cross-linked pig heart lactate dehydrogenase crystals

Carlsberg Research Communications

Volumn 41, Issue 4, 1976, Pages 211-216

  Bayne, Stephen J ^a   Ottesen, Martin ^a  

^a CARLSBERG LABORATORY   (Denmark)

Author keywords

amino acid composition; cross linked crystals; Lactate dehydrogenase; urea

Indexed keywords

EID: 0342723894     PISSN: 01051938     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02906543     Document Type: Article

References (16)

1. Spectrophotometric determination of tryptophan and tyrosine in proteins
2. The reaction of imidoesters with proteins and related small molecules
3. Molecular weight and quaternary structure of lactic dehydrogenase
4. Catalytic activity of chymotrypsin in the crystalline state
5. Hydrolysis of proteins with toluene sulphonic acid. Determination of tryptophan
6. Detection of absorption changes of pig heart lactate dehydrogenase in the wavelength range between 260 nm and 320 nm on ternary complex formation with NAD+ and oxalate
7. The activity of papain in the crystalline state
8. The physical state dependence of carboxypeptidase Aα and Aγ kinetics
9. Reactions of the cyanate present in aqueous urea with amino acids and proteins
10. Studies on the carbamylation of subtilisin type Novo
11. Effect of crystallisation on the reactivity of horse liver alcohol dehydrogenase
12. A comparative study of the thermal denaturation parameters of lysozyme in the dissolved and crystalline state