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877822-89-4

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877822-89-4 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 877822-89-4 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,7,7,8,2 and 2 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 877822-89:
(8*8)+(7*7)+(6*7)+(5*8)+(4*2)+(3*2)+(2*8)+(1*9)=234
234 % 10 = 4
So 877822-89-4 is a valid CAS Registry Number.

877822-89-4Upstream product

877822-89-4Downstream Products

877822-89-4Relevant articles and documents

Characterization of polyphenol oxidase in coffee

Mazzafera, Paulo,Robinson, Simon P

, p. 285 - 296 (2000)

Polyphenol oxidase (PPO) was characterized in partially purified extracts of leaves (PPO-L) and fruit endosperm (PPO-E) of coffee (Coffea arabica L.). PPO activity was higher in early developmental stages of both leaves and endosperm of fruits. Wounding or exposure of coffee leaves to methyl jasmonate increased PPO activity 1.5-4-fold. PPO was not latent and was not activated by protease treatment. PPO activity was stimulated 10-15% with sodium dodecyl sulphate (SDS) at 0.35-1.75 mM, but at higher concentrations activities were similar to the control samples, without detergent. Prolonged incubation of extracts-with trypsin or proteinase K inhibited PPO activity but pepsin had no effect. Inhibition of PPO with proteinase K was increased in the presence of SDS. PPO activity from both tissues was optimal at pH 6-7 and at an assay temperature of 30°C. Activity was highest with chlorogenic acid as substrate with a K(m) of 0.882 mM (PPO-L) and 2.27 mM (PPO-E). Hexadecyl trimethyl-ammonium bromide, polyvinylpyrrolidone 40, cinnamic acid and salicylhydroxamic acid inhibited PPO from both tissues. Both enzymes were inactivated by heat but the activity in endosperm extracts was more heat labile than that from leaves. The apparent M, determined by gel filtration was 46 (PPO-L) and 50 kDa (PPO-E). Activity-stained SDS-polyacrylamide gel electrophoresis (PAGE) gels and WeStern blots probed with PPO antibodies suggested the existence of a 67 kDa PPO which is susceptible to proteolytic cleavage that generates a 45 kDa active form. (C) 2000 Elsevier Science Ltd.

ROLES OF o-QUINONES AND THEIR POLYMERS IN THE ENZYMIC BROWNING OF APPLES

Rouet-Mayer, Marie-Aude,Ralambosoa, Justin,Philippon, Jean

, p. 435 - 440 (2007/10/02)

Enzymic browning and the bleaching produced by the addition of ascorbic acid have been studied simultaneously in crushed apple tissue and in pure solutions of (+)-catechin and chlorogenic acid.Spectrophotocolorimetry was used to study crushed apple tissue

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