Hyperprotease-producing mutants of Bacillus subtilis.

T B Higerd; J A Hoch; J Spizizen

doi:10.1128/jb.112.2.1026-1028.1972

Home/Archive/PubMed

PubMed · 4628743

Hyperprotease-producing mutants of Bacillus subtilis.

T B Higerd·J A Hoch·J Spizizen

View original source ↗Export metadata ↓

Abstract

A number of mutants of Bacillus subtilis producing high levels of extracellular protease have been isolated. Analysis of culture supernatants of these mutants has shown that the total amount of proteolytic activity is elevated from 16- to 37-fold over the wild strain. The elevated activity was due to a simultaneous increase in both the neutral and alkaline protease. All of the mutants genetically analyzed were found linked to the argC4 marker by PBS-1 transduction analysis.

Explore related subjects

Amylases Bacillus subtilis Caseins Cell-Free System Chromosome Mapping Culture Media Edetic Acid Genetic Linkage Mutagens Mutation Nitrosoguanidines Peptide Hydrolases Transduction, Genetic Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

T B Higerd, J A Hoch, J Spizizen. 1972. Hyperprotease-producing mutants of Bacillus subtilis.. https://doi.org/10.1128/jb.112.2.1026-1028.1972

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2007

Chylous ascites secondary to hyperlipidemic pancreatitis with normal serum amylase and lipase.

A 54-year old man with a family history of hyperlipidemia was admitted with a 12 h history of severe generalized abdominal pain associated with nausea, vomiting and abdominal distension. Examination of the abdomen revealed tenderness in the periumblical area with shifting dullness. Serum pancreatic amylase was 29 IU/L and lipase 44 IU/L, triglyceride 36.28 mmol/L. Ultrasound showed ascites. CT of the abdomen with contrast showed inflammatory changes surrounding the pancreas consistent with acute pancreatitis. Ultrasound (US) guided abdomen paracentesis yielded a milky fluid with high triglyceride content consistent with chylous ascites. The patient was kept fasting and intravenous fluid hydration was provided. Meperidine was administered for pain relief. On the following days the patient's condition improved and he was gradually restarted on a low-fat diet, and fat lowering agent (gemfibrozil) was begun, 600 mg twice a day. On d 14, abdomen US was repeated and showed fluid free peritoneal cavity. The patient was discharged after 18 d of hospitalization with 600 mg gemfibrozil twice a day. At the time of discharge, the fasting triglyceride was 4.2 mmol/L. After four weeks the patient was seen in the clinic, he was well.

Amylases↗

PubMed2007

Comparative genomic analysis of the mouse and rat amylase multigene family.

The rat and mouse amylase gene families were characterized using sequence data from the UCSC genome assembly. We found that the rat genome contains one amylase-1 and two amylase-2 genes, lying close to one another on the same chromosome. Detailed analysis revealed at least six additional amylase pseudogenes in the rat genome in the region adjacent to the amylase-2 genes. In contrast, the mouse has one amylase-1 gene and five amylase-2 genes; the latter are tandemly and systematically arranged on the same chromosome and were generated by segmental duplication. Detailed analysis revealed that the mouse has two amylase pseudogenes, located 5' to the five amylase-2 segments. Thus, the amylase genes of mouse and rat tend to be amplified; the sequences of some of them are fixed while others have become pseudogenes during evolution. This is the second report of amylase genomic organization in mammals and the first in the rodents.

Amylases↗

PubMed2007

Human pancreatic digestive enzymes.

A primary function of the pancreas is to produce digestive enzymes that are delivered to the small intestine for the hydrolysis of complex nutrients. Much of our understanding of digestive enzymes comes from studies in animals. New technologies and the availability of the sequence of the human genome allow for a critical review of older reports and assumptions based on animal studies. This report updates our understanding of human pancreatic digestive enzymes with a focus on new insights into the biology of human proteases, lipases and amylases.

Amylases↗