A condenser-receiver unit.

Potempa, S. J.; Cassaretto, Frank P.

doi:10.1021/ed023p219

Cited by 12 publications

(17 citation statements)

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“…Despite the usefulness of gelatin-PAGE for studying proteinase-mediated events during various developmental, physiological and pathogenic processes, its advantages in the analysis of reversible interactions between proteinases and the protein proteinase inhibitors have not been assessed. In particular, no simple electrophoretic procedure has been proposed to study the stability of proteinase inhibitor/proteinase complexes involving members of the two important proteinase inhibitor superfamilies cystatins [ 13, 141 and serpins [15].…”

Section: Introductionmentioning

confidence: 99%

Assessing the stability of cystatin/cysteine proteinase complexes using mildly‐denaturing gelatin‐polyacrylamide gel electrophoresis

et al. 1996

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A method for assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin-polyacrylamide gel electrophoresis (gelatin-PAGE) is described. As suggested by the use of well-known cystatins (human stefins A and B, and oryzacystatins I and II) and the plant cysteine proteinase papain, the ability of cystatin/cysteine proteinase complexes to remain stable during electrophoresis is associated with the degree of affinity between the enzyme and the inhibitor (and inversely associated with the Ki values), at least with the disulfide bond-lacking cystatins. Complexes with Ki values > or = 10(-8) M (weak interactions) are partly or completely dissociated under the conditions used, while those with lower Ki values (strong interactions) remain stable. As shown by the differential effects of two plant cystatins, oryzacystatins I and II, against a cysteine proteinase present in crude (complex) extracts from a plant pest -- the two-spotted spider mite (Tetranychus urticae Koch), the gelatin-PAGE procedure is suitable for studying the ability of cystatins to form highly stable complexes with cysteine proteinases, without the need for prior purification steps. Considering the well-recognized potential of proteinase inhibitors for pest and pathogen control, this analytical approach will be useful for rapidly assessing the respective potential of various cystatins for protection of plants, animals, and humans.

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Section: Introductionmentioning

confidence: 99%

Assessing the stability of cystatin/cysteine proteinase complexes using mildly‐denaturing gelatin‐polyacrylamide gel electrophoresis

et al. 1996

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“…inhibition [19,20]. The target proteinase specificity of inhibitory serpins is determined by the nature of the reactive site peptide bond (P1-PI').…”

Section: Resultsmentioning

confidence: 99%

Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L

et al. 1995

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A squamous cell carcinoma antigen (SSCA), which is a member of the serpin family of proteinase inhibitors, was purified from sera of cancer patients. It did not inhibit serine proteinases. However, it non-competitively inhibited human cathepsin L with a K i of 0.064 nM, but not cathepsins B and H among cysteine proteinases. These results indicated that SCCA is a non-functional serpin that inhibits cathepsin L in cancer cells.

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“…[10^12]. AT and HCII are members of the serine protease inhibitor (serpin) superfamily [13,14], and these inhibitors form 1:1 complexes with thrombin that render thrombin proteolytically inactive. Once formed the complexes are cleared via the low-density lipoprotein receptor-related protein [15].…”

Section: Introductionmentioning

confidence: 99%

Effect of oligodeoxynucleotide thrombin aptamer on thrombin inhibition by heparin cofactor II and antithrombin

Holland¹,

Henry²,

Whinna³

et al. 2000

FEBS Letters

131

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Abstract`Thrombin aptamers' are based on the 15-nucleotide consensus sequence of d(GGTTGGTGTGGTTGG) that binds specifically to thrombin's anion-binding exosite-I. The effect of aptamer^thrombin interactions during inhibition by the serine protease inhibitor (serpin) heparin cofactor II (HCII) and antithrombin (AT) has not been described. Thrombin inhibition by HCII without glycosaminoglycan was decreased V Vtwo-fold by the aptamer. In contrast, the aptamer dramatically reduced thrombin inhibition by s 200-fold and 30-fold for HCII^heparin and HCII^dermatan sulfate, respectively. The aptamer had essentially no effect on thrombin inhibition by AT with or without heparin. These results add to our understanding of thrombin aptamer activity for potential clinical application, and they further demonstrate the importance of thrombin exosite-I during inhibition by HCII^glycosaminoglycans. ß

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A condenser-receiver unit.

Abstract: COMBINED condenser, adapter, and receiving A flask. Dimensions may be accommodated to macro or semi-micro scale. The side arm of the distilling flask is connected directly. The f o m with the sealedin stopcock is especially convenient for fractional distillations.

Cited by 12 publications

References 0 publications

Assessing the stability of cystatin/cysteine proteinase complexes using mildly‐denaturing gelatin‐polyacrylamide gel electrophoresis

Assessing the stability of cystatin/cysteine proteinase complexes using mildly‐denaturing gelatin‐polyacrylamide gel electrophoresis

Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L

Effect of oligodeoxynucleotide thrombin aptamer on thrombin inhibition by heparin cofactor II and antithrombin

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