+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Some characteristics of cathepsin b ec 3.4.22.1 and alpha n benzoyl arginine beta naphthylamide hydrolase from bovine lymph nodes



Some characteristics of cathepsin b ec 3.4.22.1 and alpha n benzoyl arginine beta naphthylamide hydrolase from bovine lymph nodes



Croatica Chemica Acta 53(3): 509-518



Some properties of cathepsin B and .alpha. N-benzoylarginine-.beta.-naphthylamide (BANA) hydrolase from bovine lymph nodes were studied. .alpha.-N-benzoylarginine-.beta.-naphthylamide was a sensitive substrate for both enzymes. Leucine-2-naphthylamide was cleaved only by BANA hydrolase. Degradation of low MW substrates was optimal at pH = 6.0. At this pH value, the enzymes were most stable. Cathepsin B inactivated aldolase, was inhibited by 1 .mu.M leupeptin and by thiol blocking compounds. BANA hydrolase was not inhibited by 1 .mu.M leupeptin but showed that it required thiol compounds and EDTA for full activation. BANA hydrolase is very similar or identical to cathepsin H from rat liver lysosomes.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 006440525

Download citation: RISBibTeXText


Related references

Purification and properties of alpha n benzoyl d l arginine beta naphthylamide hydrolase h of rabbit skeletal muscle a new enzyme hydrolyzing alpha n benzoyl arginine beta naphthylamide. Agricultural & Biological Chemistry 44(7): 1705-1708, 1980

Isolation of cathepsin b ec 3.4.22.1 and alpha n benzoyl arginine beta naphthylamide hydrolase by covalent chromatography on activated thiol sepharose. Croatica Chemica Acta 52(4): 411-416, 1979

Separation of a new alpha n benzoyl arginine beta naphthylamide hydrolase from cathepsin b 1 ec 3.4.22.1 purification characterization and properties of both enzymes from rabbit lung/. Journal of Biological Chemistry 253(12): 4319-4327, 1978

Alpha n benzoyl arginine 2 naphthylamide hydrolase cathepsin b 1 from rat skin part 3 substrate specificity modifier characteristics and transformation of the enzyme at acidic ph. Acta Chemica Scandinavica Series B Organic Chemistry and Biochemistry 30(1): 53-60, 1976

Regulation by reducing agents of the proteinase activity of alpha n benzoyl d l arginine beta naphthylamide hydrolase. Federation Proceedings 41(4): ABSTRACT 5101, 1982

Purification and properties of BANA hydrolase H of rabbit skeletal muscle, a new enzyme hydrolyzing .ALPHA.-N-benzoyl-arginine-.BETA.-naphthylamide. Agricultural and Biological Chemistry 44(7): 1705-1708, 1980

A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H. Biochemical Journal 227(2): 521-528, 1985

A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and 161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N --benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H. Biochemical Journal 227(2): 521-528, 1985

Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide). Biochemical Journal 222(3): 805-814, 1984

Separation of a new alpha-N-benzoylarginine-beta-naphthylamide hydrolase from cathepsin B1. Purification, characterization, and properties of both enzymes from rabbit lung. Journal of Biological Chemistry 253(12): 4319-4326, 1978

Alpha-N-Benzoylarginine-2-naphthylamide hydrolase (cathepsin BI?) from rat skin. III. Substrate specificity, modifier characteristics, and transformation of the enzyme at acidic pH. Acta Chemica Scandinavica. Series B: Organic Chemistry and Biochemistry 30(1): 53-60, 1976

Exo peptidase and endo peptidase activities of rabbit lung alpha n benzoyl l arginol beta naphthylamide hydrolase. Federation Proceedings 37(6): 1434, 1978

Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2-dipyridyl disulphide) and with a specific synthetic substrate ( N --benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide). Biochemical Journal 222(3): 805-814, 1984

Sodium benzoyl dl arginine beta naphthylamide degrading activity in cucurbita moschata. Plant Physiology 72(Suppl. 1): 100, 1983

Degradation of lens crystallins by benzoyl-arginine-naphthylamide cleavage activity in the bovine iris and ciliary body. Nippon Ganka Gakkai Zasshi 87(11): 1212-1215, 1983