Inhibitors in amphibian morphogenesis: Enzymic degradation of an inhibitor for the vegetalizing factor

Development ◽  
1972 ◽  
Vol 28 (1) ◽  
pp. 77-86
Author(s):  
J. Born ◽  
H. Tiedemann ◽  
H. Tiedemann
Keyword(s):  
Proteolytic Enzyme ◽  
Streptomyces Griseus ◽  
Ribonuclease T1 ◽  
Pancreatic Ribonuclease ◽  
Naturally Occurring ◽  
Vegetalizing Factor

A naturally occurring inhibitor for the vegetalizing inducing factor has been incubated with different enzymes. Pancreatic ribonuclease, ribonuclease-T1, deoxyribunuclease, neuraminidase as well trypsin and papain diminish the inhibitor only very slightly or not at all. Pronase, a proteolytic enzyme from Streptomyces griseus inactivates the inhibitor completely.

scholarly journals The nucleotide sequence of cysteine transfer ribonucleic acid from baker's yeast. Products of complete digestion with pancreatic ribonuclease and ribonuclease T1

1976 ◽  
Vol 153 (2) ◽  
pp. 437-446 ◽  
Author(s):  
N J Holness ◽  
G Atfield
Keyword(s):  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Brief Treatment ◽  
Ribonuclease T1 ◽  
Pancreatic Ribonuclease ◽  
Adenylic Acid ◽  
Complete Digestion ◽  
Conventional Methods

1. The nucleotide chain of tRNA Cys from baker's yeast was readily split at the anticolon into two large fragments by brief treatment with ribonuclease T1.2. The whole molecule and the two derived large fragments were completely digested with (a) pancreatic ribonuclease and (b) ribonuclease T1. The fragments present in each of the digests were separated and sequenced by conventional methods. 3. The groups of fragments derived from the two methods of digestion were entirely compatible with each other. 4. The molecule is 75 nucleotides long, but, as isolated, lacks the terminal adenosine and the neighboring cytidylic acid residue. The minor nucleotides 1-methyladenylic acid, 7-methylguanylic acid, 5-methylcytidylic acid and N6 (γγ-dimethylallyl)adenylic acid (isopentenyladenylic acid) were identified.

scholarly journals The specificity of proteinases from Streptomyces griseus (pronase)

1970 ◽  
Vol 116 (1) ◽  
pp. 19-25 ◽  
Author(s):  
Moshe Trop ◽  
Yehudith Birk
Keyword(s):  
Streptomyces Griseus ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Considerable Extent ◽  
Small Peptides ◽  
Diisopropyl Phosphorofluoridate ◽  
Naturally Occurring ◽  
Bovine Trypsin ◽  
Wide Range ◽  
Pancreatic Trypsin Inhibitor

Purification of pronase by ion-exchange chromatography gave four proteolytically active fractions. Fraction A2 contained an endopeptidase that attacks poly l-valine. Fraction B contained an endopeptidase, an aminopeptidase and carboxypeptidases. The activities against hippuryl-L-arginine and hippuryl-L-phenylalanine could be inhibited to a considerable extent by di-isopropyl phosphorofluoridate and by EDTA. Fraction C contained an endopeptidase resembling bovine trypsin. The pure enzyme was completely inactivated by di-isopropyl phosphorofluoridate and pancreatic trypsin inhibitor and to about 90% by other naturally occurring trypsin inhibitors. Fraction D contained an apparently homogeneous endopeptidase, inhibited by diisopropyl phosphorofluoridate, that adsorbed to and hydrolysed elastin. The activity of all these fractions was tested qualitatively against a wide range of small peptides and synthetic substrates.

A PROTEOLYTIC ENZYME OF STREPTOMYCES GRISEUS

1960 ◽  
Vol 48 (3) ◽  
pp. 453-462 ◽  
Author(s):  
MASAO NOMOTO ◽  
YOSHIKO NARAHASHI ◽  
MITSURU MURAKAMI
Keyword(s):  
Proteolytic Enzyme ◽  
Streptomyces Griseus

A PROTEOLYTIC ENZYME OF STREPTOMYCES GRISEUS

1960 ◽  
Vol 48 (4) ◽  
pp. 593-602 ◽  
Author(s):  
MASAO NOMOTO ◽  
YOSHIKO NARAHASHI ◽  
MITSURU MURAKAMI
Keyword(s):  
Proteolytic Enzyme ◽  
Streptomyces Griseus

Efficient production of nonactin by Streptomyces griseus subsp. griseus

2016 ◽  
Vol 62 (8) ◽  
pp. 711-714 ◽  
Author(s):  
Yulian Zhan ◽  
Shaolun Zheng
Keyword(s):  
Chemical Synthesis ◽  
Streptomyces Griseus ◽  
Fermentation Medium ◽  
Ion Selective Electrodes ◽  
Efficient Production ◽  
Antitumor Activities ◽  
Naturally Occurring ◽  
Rotary Shaker ◽  
Means Of Production

Here we report the production of the cyclic macrotetrolide nonactin from the fermentation culture of Streptomyces griseus subsp. griseus. Nonactin is a member of a family of naturally occurring cyclic ionophores known as the macrotetrolide antibiotics. Our fermentation procedure of Streptomyces griseus was performed at 30 °C and 200 rev·min−1 for 5 days on a rotary shaker. Diaion HP-20 and Amberlite XAD-16 were added to the fermentation medium. Isolated yield of nonactin was up to 80 mg·L−1 using our methodology. Nonactin is commonly known as an ammonium ionophore and also exhibits antibacterial, antiviral, and antitumor activities. It is also widely used for the preparation of ion-selective electrodes and sensors. Chemical synthesis of nonactin has been achieved by some groups; however, overall yields are very low, making efficient biosynthesis an attractive means of production.

A Proteolytic Enzyme of Streptomyces Griseus

1959 ◽  
Vol 46 (5) ◽  
pp. 653-667 ◽  
Author(s):  
Masao Nomoto ◽  
Yoshiko Narahashi
Keyword(s):  
Proteolytic Enzyme ◽  
Streptomyces Griseus
Sign in / Sign up

Export Citation Format

Share Document