A study of two yeast proteinases.
نویسنده
چکیده
Autolysis is a procedure frequently employed in the isolation of materials from yeast. Although the intracellular yeast proteinases play an important r81e in autolysis, these enzymes have not been characterized by using up to date methods of analysis, and the existing literature concerning yeast proteinases presents conflicting results. In 1917, Dernby (1) reported that yeast contains two proteinases, a ‘Lpepsin” and a “tryptase.” The presence of two proteinases was indicated mainly by the fact that a yeast autolysate showed two pH optima for gelatin liquefaction; namely, at pH 4.5 and pH 7.0. In 1926-28, Grassmann, Willstltter, and coworkers published a series of papers on the proteolytic activity of yeast (2-4). These authors concluded that there is only one proteinase in yeast. This enzyme was reputed to be of the papain type with an optimal pH of 5.0 as measured by an alcoholic KOH titration of gelatin hydrolysis (4). However, in 1936, Hecht and Civin (5) claimed that yeast contains a “pepsin” which displays optimal activity at pH 1.8. In the present paper, the separation and partial characterization of two individual yeast proteinases are described. One has an optimal pH of about 3.7 and is rapidly denatured by urea. The other has optimal activity at pH 6.2 and may be activated by concentrated urea solutions.
منابع مشابه
Bivalent DNA Vaccination with Genes Encoding Leishmania major Cysteine Proteinases Type I and II Protects Mice Against Infectious Challenge
متن کامل
Proteinase Mutants of Saccharomyces Cerevisiaei
Fifty-nine mutants with reduced ability to cleave the chymotrypsin substrate N-acetyl-DL-phenylalanine P-naphthyl ester have been isolated in S. cerevisiae. All have reduced levels of one o r more of the three well-characterized proteinases in yeast. All have reduced levels of proteinase C (carboxypeptidase Y). These mutations define 16 complementation groups. HREE proteinases that have been ch...
متن کاملA New Approach to Virulence Factors of Candida albicans: From Gene to Function
Recently, there is an increasing trend in the diversity of pathogenic yeasts isolated from clinical samples. However, Candida albicans is even now the major cause of yeast infections. Candida albicans is one of the members of the mucosal microbiota which can cause cutaneous, mucosal, and disseminated invasive infections in susceptible individuals. For persistence in the host, the yeast must hav...
متن کاملHuman autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy.
We have cloned four human cDNAs encoding putative cysteine proteinases that have been tentatively called autophagins. These proteins are similar to Apg4/Aut2, a yeast enzyme involved in the activation of Apg8/Aut7 during the process of autophagy. The identified proteins ranging in length from 393 to 474 amino acids also contain several structural features characteristic of cysteine proteinases ...
متن کاملPhysicochemical and Rheological Properties of Toast Bread Baked by Yeast–Salt Method
Baked goods are among the most important sources of human food. They may suffer from a limited shelf life due to use of low-quality wheat. However, there are a number of novel dough preparation methods that can improve bread quality. The current study analyzed the effect of the yeast-salt method on the physicochemical and rheological properties of toast dough and bread. Baker’s yeast was used a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Journal of biological chemistry
دوره 221 2 شماره
صفحات -
تاریخ انتشار 1956