EurekaMag.com logo
+ Translate

Specificity of thermophilic streptomyces rectus var proteolyticus alkaline proteinase ec 3.4.21.14


, : Specificity of thermophilic streptomyces rectus var proteolyticus alkaline proteinase ec 3.4.21.14. Agricultural and Biological Chemistry 46(10): 2485-2490

The specificity of highly purified alkaline proteinase B (EC 3.4.21.14) from thermophilic S. rectus var. proteolyticus was investigated with an oxidized insulin B chain. Hydrolysis of the oxidized insulin B chain in a 4 h incubation was observed mainly at 3 peptide bonds (Phe24-Phe25, Leu15-Tyr16 and Leu11-Val12) and additionally at 6 others (Leu6-CySO3H7, Gln4-His5, Leu17-Val18, His5-Leu6, Glu13-Ala14, Asn3-Gln4). Hydrolysis of angiotensin (formerly designated angiotensin II) was observed at the Tyr4-Ile5 bond. Hydrolysis of proangiotensin (formerly designated angiotensin I) was observed at the Tyr4-Ile5 and Phe8-His9 bonds.

(PDF 0-2 workdays service)

Accession: 006459149

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Mizusawa, K.; Ichishima, E.; Yoshida, F., 1969: Production of thermo stable alkaline enz proteases by thermophilic streptomyces streptomyces rectus var proteolyticus enz alkaline proteinase enz carboxy peptidase. Applied Microbiology 17(3): 366-371

Mizusawa, K.; Yoshida, F., 1976: Role of sulfhydryl group in the structure and function of alkaline proteases from a thermophilic actinomycete, Streptomyces rectus var. proteolyticus. Experientia. Supplementum 26: 61-66

Mizusawa K.; Yoshida F., 1976: Role of a sulfhydryl group in the structure and function of alkaline proteases from a thermophilic actinomycete streptomyces rectus var proteolyticus. Zuber, Herbert (Ed ) Experientia Supplementum, Vol 26 Enzymes And Proteins From Thermophilic Microorganisms Structure And Function Proceedings Of The International Symposium Zurich, Switzerland, July 28-Aug 1, 1975 445p Illus Birkhauser Verlag: Basel, Switzerland Isbn 3-7643-0827-3 61-66

Mizusawa, K.; Yoshida, F., 1972: Thermophilic Streptomyces alkaline proteinase. I. Isolation, crystallization, and physicochemical properties. Journal of Biological Chemistry 247(21): 6978-6984

Mizusawa, K.; Yoshida, F., 1972: Thermophilic streptomyces alkaline proteinase part 1 isolation crystallization and physicochemical properties. Journal of Biological Chemistry 247(21): 6978-6984

Mizusawa, K.; Yoshida, F., 1973: Thermophilic Streptomyces alkaline proteinase. II. The role of a sulfhydryl group and the conformational stability. Journal of Biological Chemistry 248(12): 4417-4423

Mizusawa, K.; Yoshida, F., 1973: Thermophilic streptomyces alkaline proteinase part 2 the role of a sulfhydryl group and the conformational stability. Journal of Biological Chemistry 248(12): 4417-4423

Ichishima, E.M.tsue, M., 1981: Initial site of cleavage towards oxidized B-chain of insulin by thermophilic Streptomyces alkaline proteinase. Current microbiology(1): 17-20

Tanaka, T.; Matsuzawa, H.; Ohta, T., 1998: Substrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1: Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg. Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we c...

Tanaka, T.; Matsuzawa, H.; Ohta, T., 1998: Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: Comparison with proteinase K, subtilisin BPN' and subtilisin Carlsberg. Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we c...