Further studies on ε-lysine acylase. The ω-N-acyl-diamino acid hydrolase activity of avian kidney

1968 ◽  
Vol 46 (5) ◽  
pp. 471-475 ◽  
Author(s):  
Jean Leclerc ◽  
Leo Benoiton
Keyword(s):  
Hydrolase Activity ◽  
Acid Hydrolase ◽  
Enzyme Preparations ◽  
Kidney Enzyme ◽  
Diamino Acid ◽  
Avian Kidney ◽  
Derivatives Of ◽  
Hog Kidney

ω-N-Acyl-diamino acids have been tested as substrates for ε-lysine acylase from animal sources. Chicken and pigeon kidney enzyme preparations hydrolyzed derivatives of lysine homologues as well as of lysine, the best substrates tested being ε-N-propionyl-lysine and ε-N-propionyl-ornithine. A modified procedure for purifying the enzyme from rat and hog kidney is presented. Some of its properties are different from those previously reported.

Acid Hydrolase Activity in Osteoarthritic and Normal Human Cartilage

1973 ◽  
Vol 55 (5) ◽  
pp. 1068-1076 ◽  
Author(s):  
MICHAEL G. EHRLICH ◽  
HENRY J. MANKIN ◽  
BENJAMIN V. TREADWELL
Keyword(s):  
Hydrolase Activity ◽  
Acid Hydrolase ◽  
Human Cartilage ◽  
Normal Human

Hydroxycinnamoyl: Coenzyme A Transferase Involved in the Biosynthesis of Kaempferol-3-(p-coumaroyl Triglucoside) in Pisum sativum

1977 ◽  
Vol 32 (9-10) ◽  
pp. 765-768 ◽  
Author(s):  
Marie H. Saylor ◽  
Richard L. Mansell
Keyword(s):  
Coenzyme A ◽  
Chemical Properties ◽  
Acyl Donor ◽  
Coumaric Acid ◽  
Enzyme Preparations ◽  
Naturally Occurring ◽  
Enzymatic Formation ◽  
Derivatives Of ◽  
Acid Esters ◽  
And Chemical Properties

Abstract The major flavonoids of Pisum are derivatives of kaempferol and quercetin, including both tri-glucosides and acylated triglucosides in which the acyl group is p-coumaric acid. Although hydroxy-cinnamic acid esters of flavonoids are common pigments in many plants, neither the enzymes nor the precursors involved in their biosynthesis have been demonstrated. We report here that crude enzyme preparations extracted from peas catalyze the transfer of the p-coumaroyl moiety of p-coumaroyl: Coenzyme A to kaempferol-3-triglucoside forming kaempferol-3-(p-coumaroyl triglucoside) as the acylated product. The reaction product has been vigorously shown to be identical to the naturally occurring kaempferol-3-(p-coumaroyl triglucoside) in both chromatographic and chemical properties. The enzymatic formation of the acylated derivative occurred only minimally when incubated with the cofactors required for carboxyl group activation (ligase) and maximally when incubated with p-coumaroyl : Coenzyme A as the acyl donor.

Investigation of serum acid hydrolase activity in immunodepression

1984 ◽  
Vol 97 (4) ◽  
pp. 458-460
Author(s):  
V. A. Drozhennikov ◽  
O. S. Belorusov ◽  
S. T. Tsygankova ◽  
M. M. Kapichnikov ◽  
Yu. V. Zykov ◽  
...  
Keyword(s):  
Hydrolase Activity ◽  
Acid Hydrolase

scholarly journals STUDIES ON LYSOSOMES

1968 ◽  
Vol 37 (2) ◽  
pp. 394-411 ◽  
Author(s):  
Günter Brittinger ◽  
Rochelle Hirschhorn ◽  
Steven D. Douglas ◽  
Gerald Weissmann
Keyword(s):  
Acid Phosphatase ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Structural Characteristics ◽  
Gradient Centrifugation ◽  
Human Lymphocytes ◽  
Peripheral Blood Lymphocytes ◽  
Hydrolase Activity ◽  
Cell Fractionation ◽  
Acid Hydrolase

Pure suspensions of human lymphocytes were separated from peripheral blood by means of nylon wool, homogenized in 0.34 M sucrose-0.01 M EDTA solution, and fractionated by differential centrifugation. The bulk of acid hydrolase activity was found to be concentrated in a 20,000 g x 20 min granular fraction, whereas nuclear, debris, and supernatant fractions contained lesser concentrations of hydrolases. Acid hydrolase activity present in the granular fraction showed appropriate "latency" as judged by its dose-dependent release into the 20,000 g x 20 min supernatant after exposure to membrane-disruptive agents such as streptolysin S, filipin, and lysolecithin. Heparin proved to be necessary in the suspending medium so that reproducible homogenization and cell fractionation could be obtained. Even excessive contamination of lymphocyte suspensions with platelets did not appreciably alter the acid hydrolase activity of lymphocyte homogenates or the distribution of enzymes in subcellular fractions. Discontinuous density-gradient centrifugation of a 500 g x 10 min supernatant, containing both acid hydrolase-rich organelles and mitochondria, resulted in partial resolution of hydrolase-rich organelles from mitochondria. Fine structural studies of the intact lymphocytes showed the presence of acid phosphatase-positive, membrane-bounded organelles. Electron microscopy of the "large granule" (20,000 g x 20 min) fraction of such lymphocytes demonstrated 80–90% mitochondria, 5–10% platelets, and 5–10% membrane-bounded acid phosphatase-positive structures. The data indicate the presence in human peripheral blood lymphocytes of acid hydrolase-rich granules which possess many of the biochemical and structural characteristics of lysosomes in other tissues.

The action of some enzymes on homolysine derivatives

1968 ◽  
Vol 46 (4) ◽  
pp. 387-389 ◽  
Author(s):  
John H. Seely ◽  
Leo Benoiton
Keyword(s):  
Amino Acid ◽  
Ethyl Ester ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Lysine Decarboxylase ◽  
Amino Acid Oxidase ◽  
Kidney Enzyme ◽  
Chicken Kidney ◽  
Hog Kidney

DL-Homolysine was resistant to the action of lysine decarboxylase from Bacterium cadaveris, but was oxidized by L-amino acid oxidase from Crotalus adamanteus. ε-N-Acetyl-DL-homolysine was not hydrolyzed by ε-lysine acylase from hog kidney, but was hydrolyzed by a chicken kidney enzyme preparation. Hog kidney acylase showed slight activity towards α-N,ζ-N-dichloroacetyl- and α-N-chloroacetyl-ζ-N-carbobenzoxy-DL-homolysine. DL-Homolysine ethyl ester was hydrolyzed by trypsin at a rate one-eighth of that for lysine ethyl ester.

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