Carlsberg protein

McPhalen, C. A., James, M. N. G. Structural comparison of two serine proteinase-protein inhibitor complexes Eglin-C-Subtilisin Carlsberg and CI-2-subtilisin novo. Biochemistry 27 (1988) 6582-6598... 

Scheraga, H. A., Protein structure and function, from a colloidal to a molecular view, Carlsberg Res. Comm., 49, 1, 1984. 

Characterisation of two Water-Soluble High-Lysine Protein Carlsberg Res. Commun, 45, 47-58... 

For single-tryptophan proteins there is some correlation between blue-shifted fluorescence emission maximum and phosphorescence lifetime (Table 3.2). Another correlation is that three of the proteins which exhibit phosphorescence, azurin, protease (subtilisin Carlsberg), and ribonuclease Tlt are reported to show resolved fluorescence emission at 77 K. Both blue-shifted emission spectra and resolved spectra are characteristic of indole in a hydrocarbon-like matrix. 

F. M. Richards, Packing defects, cavities, volume fluctuations and access to the interior of proteins, Carlsberg Res. Commun. 44, 47-63 (1979). 

The hbraries of enzyme substrates were obtained by spht-pool synthesis to yield one-bead-one-compound hbraries. The substrate assay was performed with a range of proteolytic enzymes such as subtilisin Carlsberg [26], cruzipain [27], protein disulfide isomerase [28-29], matrix metalloprotease MM P-9 [30], papain [31],... 

Tincture of the dried seed, on agar plate at a concentration of 30 p,L/disc, was inactive on Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Extract of 10 g plant material in 100 mL ethanol was used b Anticoagulation activity. Serpin BSZx (an inhibitor of trypsin and chemotrypsin) inhibited thrombin, plasma kallikrein, factor Vlla/tissue factor, and factor Xa at heparin-independent association rates. Only factor Xa turned a significant fraction of BSZx over as substrate. Activated protein C and leukocyte elastase were slowly inhibited by BSZx, whereas factor Xlla, urokinase and tissue type plasminogen activator, plasmin and pancreas kallikrein, and elastase were not or only weakly affected. Trypsin from Fusarium was not inhibited, while interaction with subtilisin Carlsberg and Novo was rapid, but most BSZx was cleaved as a substrate L... 

Asano, K., B. Svensson, and F. M. Polsen. Isolation and characterization of inhibitors of animal cell-free protein synthesis from barley seeds. Carlsberg Res Commun 1984 49(7) 619—626. Roberts, W. K., and C. P. Selitren-nikoff. Isolation and partial characterization of two antifungal proteins from barley. Biochim Biophys Acta 1986 880 161-170. 

When 18-crown-6 was co-lyophilized with a-chymotrypsin, a 470-fold activation was seen over the free enzyme in the transesterification of APEE with 1-propanol in cyclohexane (Scheme 3.2) [96]. There was a low apparent specificity for the size and macrocyclic nature of the crown ether additives, suggesting that, during lyophilization, 18-crown-6 protects the overall native conformation and acts as a lyoprotectant. To examine this global effect, FTIR was used to examine the effect of crown ethers on the secondary structure of enzymes. In one study [98], subtilisin Carlsberg was shown to retain its secondary structure in 1,4-dioxane when lyophi-lized in a 1 1 ratio with 18-crown-6. In addition, examination of FTIR spectra from varying incubation temperatures indicated that an increase in crown ether content in the final enzyme preparation resulted in a decreased denaturation temperature in the solvent, indicating a more flexible protein structure. 

Fig. 6. Hydration surface dynamics of the protein (enzyme) Substilisin Carlsberg, and for comparison that of bulk water, and a probe outside the water layer...

The new generations of experiments are aimed at linking dynamical studies of these and other processes to the function. We have already begun research in this direction. In a recent publication [9] we reported studies of the femtosecond dynamics of an RNA-protein complex and then compared the results with those obtained for in vivo (E. Coli) transcription anti-termination activities. In two other studies we measured the activity of the protein Subtilisin Carlsberg, discussed above, to a substrate, and the role of hydration in interfacial binding and function of bovine pancreatic phospholipase at a substrate site. The goal in all these studies is to relate structures to the dynamics and hopefully to key features of the (complex ) function. 

Bassi, R., Machold O. and Simpson D.J. 1985. Chlorophyll-proteins of two photosystem I preparations from maize. Carlsberg Res. Commun. 50,145-162. 

Simpson, D.J. 1979. Freeze-fracture studies on barley plastid membranes. III. Location of the light-harvesting chlorophyll-protein. Carlsberg Res. Commun. 44, 305-336. 

The alkaline serine protease of Bacillus licheniformis, also known as Subtilisin Carlsberg, is the preferred protease in most nonionic and anionic detergents. It attacks many peptide bonds and easily dissolves proteins. It may be used at temperatures up to 65°C, and its pH optimum is close to 9.0, the pH normally used in washing fluids. 

If younger readers are unaware of the traditions of purificadon of proteins, especially those established in the Carlsberg Laboratory and the former Department of Physical Chemistry at Harvard Medical School, and the rewards for the sheer hard work involved in isolation, we refer them to the recent autobiography of Arthur Kornberg (1989). 

G66. Gregory, M. E., Holdsworth, E. S., and Ottesen, M., Some properties of a clinically active cyanocobalamin-protein complex. Compt. Rend. Trav. Lab. Carlsberg Ser. Chim. 30, 147-155 (1957). 

Modification of Ultrafiltered versus Acid Precipitated Soy Protein. When the retentate obtained from the ultrafiltration of soybean extract is subjected to an enzymatic hydrolysis as described earlier (2) for acid precipitated protein, a hydrolysis curve (DH versus time) may be drawn. A comparison of such hydrolysis curves is shown in Fig. 2 for acid precipitated soy protein isolate and ultrafiltered soy protein isolate. The curves are drawn on the basis of the same hydrolysis parameters. The enzyme used is the microbial alkaline protease subtilisin Carlsberg (ALCALASE ). 

It appears from Fig. 2 that the ultrafiltered soy protein isolate is hydrolyzed considerably more slowly than the acid precipitated protein. This is due to the compact molecular structure of the ultrafiltered protein, which is still in the native state. That the degree of denaturation of a protein substrate has a profound influence on the kinetics of the proteolysis has been known for long, see Christensen W. It should be noted that subtilisin Carlsberg is not inhibited by the protease inhibitors present in native bean protein (7 ). 

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