scholarly journals THE ENZYMATIC HYDROLYSIS OF AMINO ACID β-NAPHTHYLAMIDES: I. PREPARATION OF AMINO ACID AND DIPEPTIDE β-NAPHTHYLAMIDES

1965 ◽  
Vol 13 (1) ◽  
pp. 57-64 ◽  
Author(s):  
G. G. GLENNER ◽  
L. A. COHEN ◽  
J. E. FOLK
Keyword(s):  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Biochemical Systems ◽  
Hydrolysis Of ◽  
Acid Salts

The acid salts of amino acid β-naphthylamides have been found to have greater stability and solubility than their corresponding free bases. For the purpose of applying these substrates in subsequent studies in histochemical and biochemical systems, the syntheses and characteristics of a large variety of previously unreported intermediates, acid salts and free bases of amino acid β-naphthylamides and their analogues are described.

Synthesis and enzymatic hydrolysis of aspirin-basic amino acid ethyl esters

1991 ◽  
Vol 68 (1-3) ◽  
pp. 77-86 ◽  
Author(s):  
Tsunematsu Hideaki ◽  
Ishida Eiji ◽  
Yoshida Shiro ◽  
Yamamoto Magobei
Keyword(s):  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Basic Amino Acid ◽  
Ethyl Esters ◽  
Hydrolysis Of

Synthesis and the Stereoselective Enzymatic Hydrolysis of Flurbiprofen-Basic Amino Acid Ethyl Esters

1995 ◽  
Vol 2 (6) ◽  
pp. 517-525 ◽  
Author(s):  
Hideaki Tsunematsu ◽  
Shiro Yoshida ◽  
Kenichi Horie ◽  
Magobei Yamamoto
Keyword(s):  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Basic Amino Acid ◽  
Ethyl Esters ◽  
Hydrolysis Of

Novel betaine-amino acid based natural deep eutectic solvents for enhancing the enzymatic hydrolysis of corncob

2020 ◽  
Vol 310 ◽  
pp. 123389 ◽  
Author(s):  
Yuan Liang ◽  
Wenjing Duan ◽  
Xiaoxi An ◽  
Yingyun Qiao ◽  
Yuanyu Tian ◽  
...  
Keyword(s):  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Deep Eutectic Solvents ◽  
Natural Deep Eutectic Solvents ◽  
Hydrolysis Of

New insight into enzymatic hydrolysis of peptides with site-specific amino acid d-isomerization

2020 ◽  
Vol 105 ◽  
pp. 104389
Author(s):  
Liang Yan ◽  
Yongqi Ke ◽  
Yuhe Kan ◽  
Dao Lin ◽  
Jingkui Yang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Enzymatic Hydrolysis ◽  
Site Specific ◽  
Specific Amino Acid ◽  
Hydrolysis Of ◽  
Insight Into

scholarly journals THE ENZYMATIC HYDROLYSIS OF AMINO ACID β-NAPHTHYLAMIDES II. PARTIAL PURIFICATION AND PROPERTIES OF A PARTICLE-BOUND COBALT-ACTIVATED RAT KIDNEY AMINOPEPTIDASE

1966 ◽  
Vol 14 (5) ◽  
pp. 401-413 ◽  
Author(s):  
K. FELGENHAUER ◽  
G. G. GLENNER
Keyword(s):  
Amino Acid ◽  
Rat Kidney ◽  
Deae Cellulose ◽  
Enzymic Activity ◽  
Disc Electrophoresis ◽  
Partial Purification ◽  
Soluble Enzyme ◽  
Solvent Fractionation ◽  
Biochemical Systems ◽  
Hydrolysis Of

In order to determine the relationship and characteristics of the soluble and tissue-bound (so-called "lyo" and "desmo") components of enzymes in histochemical and biochemical systems, a biochemical investigation of the hydrolysis of l-leucyl β-naphthylamide in rat kidney was undertaken. By ultracentrifugation, autolysis, salt and solvent fractionation procedures and DEAE-cellulose column chromatography primary soluble and tissuue-bound enzymes were separated and partially purified. The soluble enzyme was found to be inhibited by p-chloromercuribenzoate and reactivated by cysteine. The tissue-bound enzyme was found to be inhibited by o-phenanthroline and reactivated by Co++, and hydrolyzed peptides and amino acid β-naphthylamides at rates differing markedly from those of the soluble enzyme and commercial leucine aminopeptidase. Disc electrophoresis of the tissue-bound enzyme preparation demonstrated two protein bands, both revealing enzymic activity with almost identical hydrolytic characteristics, i.e., isozymes. This evidence established the identity of the tissue-bound Co++-activated enzyme with that found histochemically in the brush border of the proximal tubuli, and indicated its functional capacity as that of an aminopolypeptidase. It was also concluded that in the system investigated the "lyo" and "desmo" components represented, in reality, distinct enzymes with unique characteristics.

Sign in / Sign up

Export Citation Format

Share Document