| 1. |
- Abrahamson, Magnus, et al.
(författare)
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Human cystatin C: Role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase
- 1991
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Ingår i: Biochemical Journal. - 0264-6021. ; 273:3, s. 621-626
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Tidskriftsartikel (refereegranskat)abstract
- Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the human cysteine-proteinase inhibitor cystatin C at neutral pH. The resulting modified inhibitor had size and amino acid composition consistent with a cystatin C molecule devoid of the N-terminal Ser-1-Val-10 decapeptide. Leucocyte-elastase-modified cystatin C had more than 240-fold lower affinity than native cystatin C for papain. Removal of the N-terminal decapeptide of human cystatin C also decreased inhibition of human cathepsins B and L by three orders of magnitude, but decreased inhibition of cathepsin H by only 5-fold. A tripeptidyldiazomethane analogue of of the N-terminal portion of cystatin C was a good inhibitor of cathepsins B and L but a poor inhibitor of cathepsin H. It therefore appears that amino acid side chains of the N-terminal segment of cystatin C bind in the substrate-binding pockets of cathepsins B and L but not in those of cathepsin H. It is argued that the N-terminal cystatin C interaction with cathepsin B is physiologically important and hence that leucocyte elastase could have a function as a regulator of extracellular cysteine-proteinase inhibitory activity at sites of inflammation.
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| 2. |
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| 3. |
- Abrahamsson, Sven Olof, et al.
(författare)
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Dehydration inhibits matrix synthesis and cell proliferation : An in vitro study of rabbit flexor tendons
- 1991
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Ingår i: Acta Orthopaedica. - : Medical Journals Sweden AB. - 1745-3674 .- 0001-6470. ; 62:2, s. 159-162
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Tidskriftsartikel (refereegranskat)abstract
- Segments of the deep flexor tendon of the rabbit were exposed to air; the effects of dehydration on in vitro synthesis of proteoglycan, collagen, non-collagenous protein, and cell proliferation were compared with tendon segments that were kept moist with physiologic saline. After 20 min of expo-sure to air, the tendons lost half and after 40 min all of their ability to synthesize matrix components and to proliferate, whereas irrigated tendons remained viable during the entire experiment.
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| 4. |
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| 5. |
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| 6. |
- Adlercreutz, Patrick
(författare)
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Asymmetric reduction of ketones with enzymes from acetic acid bacteria
- 1991
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Ingår i: Biotechnology Letters. - 0141-5492. ; 13:4, s. 229-234
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Tidskriftsartikel (refereegranskat)abstract
- Six strains of acetic acid bacteria were evaluated with respect to their capability to catalyze the stereoselective reduction of ketones. The cells were permeabilized before the bioconversions. The best strains were Gluconobacter oxydans DSM 50049 and Acetobacter aceti DSM 2002. Using either of these two strains it was possible to reduce all 12 ketones to (S)-alcohols with an enantiomeric excess of ≥94 %. The highest level of enzymatic activity was found in Acetobacter aceti DSM 2002.
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| 7. |
- Adlercreutz, P., et al.
(författare)
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Catalytic properties of α-chymotrypsin in organic media
- 1991
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Ingår i: Biomedica Biochimica Acta. - 0232-766X. ; 50:10-11, s. 55-60
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Tidskriftsartikel (refereegranskat)abstract
- α-Chymotrypsin was deposited on Celite and the resulting immobilized preparations were used to carry out peptide synthesis reactions in organic media with only small amounts of water present. The influence of different parts of the donor ester and acceptor nucleophile substrate molecules on the kinetics of the enzymatic reactions was studied. The specificity of α-chymotrypsin in organic media was a combination of its substrate specificity in aqueous media and solvent effects. The kinetics of peptide synthesis can thus be modulated by using suitable solvents and protecting groups.
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| 8. |
- Adlercreutz, Patrick
(författare)
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Novel biocatalyst for the asymmetric reduction of ketones : Permeabilized cells of Gluconobacter oxydans
- 1991
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Ingår i: Enzyme and Microbial Technology. - : Elsevier BV. - 0141-0229. ; 13:1, s. 9-14
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Tidskriftsartikel (refereegranskat)abstract
- Gluconobacter oxydans (ATCC 621) were permeabilized with toluene and then lyophilized. This crude enzyme preparation was used to reduce eleven ketones to (S)-alcohols with high enantiomeric excess (for most alcohols 93%-99% e.e.). The coenzyme NADH was regenerated either by adding a second enzyme, formate dehydrogenase, and its substrate, formate, or with 2-butanol as a second substrate for the G. oxydans enzyme(s). With the first of these methods, almost complete conversion was achieved. Permeabilized cells immobilized in calcium alginate gel were used for 18 days without any significant loss of catalytic activity.
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| 9. |
- ADLERCREUTZ, Patrick
(författare)
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On the importance of the support material for enzymatic synthesis in organic media : Support effects at controlled water activity
- 1991
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 199:3, s. 609-614
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Tidskriftsartikel (refereegranskat)abstract
- Enzymes were deposited on different porous support materials and these preparations were used to catalyze reactions in organic media. Reactions were carried out at specific water activities, achieved by equilibrating both the enzyme preparation and the substrate solution at the desired water activity before mixing them and thereby starting the reactions. The reaction rates obtained at the same water activity with different supports differed greatly, indicating a direct influence of the support on the enzyme. For horse liver alcohol dehydrogenase, Celite was the best support, and the reaction rate increased with increasing water activity. In the α‐chymotrypsin‐catalyzed alcoholysis of N‐acetyl‐l‐phenylalanine ethyl ester with 1‐butanol, high rates were again obtained with Celite, but with this support only about one third of the ethyl ester was converted to butyl ester, the rest was hydrolyzed. With the polyamide support, Accurel PA6, alcoholysis was the dominating reaction, and by using a low water activity (0.33), hydrolysis was completely suppressed while still maintaining a high alcoholysis activity. Controlled pore glass (CPG), derivatized with either hexyl or glucosyl groups, had quite different properties as enzyme supports. For horse liver alcohol dehydrogenase, glucose‐CPG was a much better support than hexyl‐CPG, and in the α‐chymotrypsin‐catalyzed reactions, glucose‐CPG favored hydrolysis, and hexyl‐CPG alcoholysis, at water activities exceeding 0.8. The results are discussed considering the absorption of water on the enzymes, on the supports and the solubility of water in the reaction media; all these parameters were measured separately.
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| 10. |
- Agardh, Carl-David, et al.
(författare)
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Association between urinary N-acetyl-beta-glucosaminidase and its isoenzyme patterns and microangiopathy in type 1 diabetes mellitus
- 1991
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Ingår i: Clinical Chemistry. - 0009-9147. ; 37:10 Pt 1, s. 1696-1699
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Tidskriftsartikel (refereegranskat)abstract
- Urinary N-acetyl-beta-glucosaminidase (NAG) and its isoenzymes (NAG A and NAG B) in samples from 87 type 1 diabetic patients and 40 apparently healthy reference subjects were studied with enzyme immunoassays. The diabetic patients had higher concentrations of urinary NAG than did the control subjects (P less than 0.01), but the isoenzyme pattern did not differ. There was a positive correlation between metabolic control (Hb A1c concentrations) and total NAG (P less than 0.01), NAG A (P less than 0.01), and NAG B (P less than 0.001). The diabetic patients were divided into three groups, depending on the degree of retinopathy. Subjects with severe forms of retinopathy did not have increased concentrations of urinary NAG unless they had concomitant nephropathy. The isoenzyme pattern was similar irrespective of degree of retinopathy or nephropathy. The results indicate that concentrations of urinary NAG are positively correlated to the degree of nephropathy, whereas there is no such correlation to the degree of retinopathy.
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