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Detail of "987-84-8"

  • CAS Number:
  • 987-84-8
  • Name:
  • L-Phenylalanine,N-[(phenylmethoxy)carbonyl]-L-a-glutamyl-

  • Molecular Structure:
  • Formula:
  • C22H24 N2 O7
  • Molecular Weight:
  • 428.44
  • Synonyms:
  • Glutaramicacid, 4-(carboxyamino)-N-(a-carboxyphenethyl)-, 4-benzyl ester, stereoisomer (7CI,8CI); L-Phenylalanine,N-[N-[(phenylmethoxy)carbonyl]-L-a-glutamyl]-; Alanine, N-carboxy-L-glutamylphenyl-, N-benzyl ester, L-(8CI); Benzyloxycarbonyl-L-glutamyl-L-phenylalanine;Carbobenzoxy-L-glutamyl-L-phenylalanine; N-(Benzyloxycarbonyl)-a-L-glutamyl-L-phenylalanine;N-Carbobenzoxy-L-glutamyl-L-phenylalanine; NSC 18760; NSC 89650
  • EINECS:
  • 213-581-2
  • Density:
  • 1.325 g/cm3
  • Boiling Point:
  • 760.4 °C at 760 mmHg
  • Flash Point:
  • 413.7 °C

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CAS No.987-84-8 Z-GLU-PHE-OH

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CAS No.987-84-8 L-Phenylalanine,N-[(phenylmethoxy)carbonyl]-L-a-glutamyl-

Supplier:AHH Chemical Co.,Ltd [ China (Mainland)]

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Reference

Partial purification and some enzymic properties of cathepsin A (F-II) from squid liver
Partial purification and some enzymic properties of cathepsin A (F-II) from squid liver. Ikeda, Eiko; Inaba, Takashi; Fujii, Minoru (Lab. Biochem., Saga Univ., Saga, Japan). Saga Daigaku Nogaku Iho, 41, 9-20 (Japanese) 1976. CODEN: SDNIA4. 988-75-0 and 987-84-8 are also occured in this study. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Cathepsin A from the liver of squid, Dorytheuthis bleederi, was sepd. into 2 active fractions, F-I and F-II, by CM-cellulose column chromatog. F-II was partially purified .apprx.100-fold. Gel filtration on Sephadex g-200 gave mol. wts. of .apprx.107,000 and 58,000 for F-I and F-II, resp. Isoelec. focusing of F-II gave an isoelec. point of pH 5.1. The enzyme was stable between pH 4.9-5.6. The optimum pH for the hydrolysis of Z-Glu-Tyr (Z = N-carbobenzoxy) was 4.6-5.2. The enzyme catalyzed the hydrolysis of dipeptide derivs., such as Z-Glu-Tyr, Z-Glu-Phe, and Z-Gly-Phe. Z-Gly-Leu and Z-Gly-Pro were hardly hydrolyzed. The values of Km for Z-Gly-Tyr and Z-Glu-Phe were 1.5 and 3.2 mM, resp., in 0.1M acetate buffer, pH 5.0, at 37.degree.. The enzyme was strongly inactivated by iodoacetic acid, HgCl2, and diisopropyl fluorophosphate at pH 5.0. No inhibition of the enzyme was obsd. in the presence of EDTA or 1,10-phenanthroline. .
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