Purification properties and specificity of cathepsin D from Cyprinus carpio

Goldman-Levkovitz, Sara; Rimon, Abraham; Rimon, Sara

doi:10.1016/0305-0491(95)00036-8

Cited by 14 publications

(11 citation statements)

References 9 publications

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“…Cathepsin D from other sources have been reported to comprise of two chains (heavy and light), linked together by disulfide bonds (Fusek et al 2013) and there is a distinct heterogeneity in the size of individual chains depending on the source (Huang et al 1979;Goldman-Levkovitz et al 1995;Fusek et al 2013). The molecular weight of pepsin reported in the present study was similar to that reported by Bohak (1969); Fox et al (1977) for chicken proventricular pepsin and sheep pepsin, respectively.…”

Section: Determination Of Purity Molecular Weight and Identificationsupporting

confidence: 84%

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Jamdar

Harikumar

2016

Journal of Food Biochemistry

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Chicken intestine, an underutilized by-product of poultry industry is a rich source of tissue proteases, especially aspartic proteases. Two of the major aspartic proteases of the tissue were purified from lysosomal and post lysosomal fractions and identified by N-terminal amino acid sequencing as cathepsin D and pepsin, respectively. The enzymes differed in their molecular and biochemical properties like molecular weight, optimum conditions for protein degradation and stability in different conditions of pH and temperature. Both enzymes were completely inhibited by pepstatin. The kinetic constant, Km for chicken intestinal pepsin and cathepsin D (for haemoglobin substrate) were estimated to be 6.45 lM and 22.7 lM, respectively. The interaction of both enzymes with different food proteins suggests pepsin could be used in applications demanding extensive hydrolysis of proteins, while cathepsin D could be used in those needing controlled degradation of proteins. PRACTICAL APPLICATIONSChicken intestine is a by-product of poultry industry. The tissue could serve as a major source of proteases especially aspartic proteases, which can be used as an alternative for proteases currently used in food industries. Aspartic proteases (pepsin and cathepsin D) from this tissue can be recovered and used for preparation of protein hydrolysates in a more economical way. Furthermore, the byproduct can be exploited to increase revenues for poultry processors.

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Section: Determination Of Purity Molecular Weight and Identificationsupporting

confidence: 84%

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Jamdar

Harikumar

2016

Journal of Food Biochemistry

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“…Barnard (1973) suggested that the cathepsin D was probably important in intracellular digestion in lower invertebrates without a well‐developed extracellular digestive system. Goldman‐Levkovitz et al. (1995) reported a cathepsin D from Cyprinus carpio whose properties and specificity were similar to those of pepsins from fish gut.…”

Section: Discussionmentioning

confidence: 92%

“…Barnard (1973) suggested that the cathepsin D was probably important in intracellular digestion in lower invertebrates without a well-developed extra- cellular digestive system. Goldman-Levkovitz et al (1995) reported a cathepsin D from Cyprinus carpio whose properties and specificity were similar to those of pepsins from fish gut. Komai et al (2004) reported a cathepsin D from the hepatopancreas of Japanese common aquid (Todarodes pacificus) whose gene was classified to pepsinsÕ cluster.…”

Section: Discussionmentioning

confidence: 92%

Partial characterization and activity distribution of proteases along the intestine of grass carp, Ctenopharyngodon idella (Val.)

Liu

Wang

et al. 2008

Aquaculture Nutrition

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A series of studies based on biochemical assays and electrophoretical observations has been conducted in order to investigate activity distributions and partially characterize various types of proteinases in the digestive tract of grass carp, Ctenopharyngodon idella (Val.). The casein digestion assays revealed that the presence of acidic proteinase had the highest activity at pH 2.5–3.0 and the alkaline proteinases at pH 10.0. The acidic proteinase activity distribution was found to decrease gradually from the oesophagus to the anus. Pepstatin A and EDTA inhibited the acidic proteinases activity. The SDS‐substrate‐PAGE showed that crude extraction of grass carp intestine contained an acidic proteinase active component with molecular mass of 28.5 ku. The substrate‐PAGE at neutral pH condition showed the presence of two acidic proteinase active components. The activity distribution of alkaline proteinase was found to slightly fluctuate along the intestine. And the whole intestine had very high activity. The inhibition assays and substrate specificity assays showed that trypsin was the main active component of the alkaline proteinases. The SDS‐substrate‐PAGE further showed that the crude extraction of grass carp intestine had four types of alkaline proteinase with molecular mass of 26.4, 30.8, 43.0 and 105.0 ku respectively. They were characterized to be trypsin (26.4, 30.8 and 43.0 ku) and un‐serine proteinase (105.0 ku) respectively. No chymotrypsin was detected.

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“…It has been shown that, in sea bass muscle, they are differently expressed depending on the season of the year (Ladrat, Chaplet, Verrez-Bagnis, Noël & Fleurence, 2000). On the other hand, cathepsins B, D, L and H are the major cathepsins within the fish lysosomes (Aoki, Yamashita & Ueno, 2000) ; some of them have been studied for their enzymatic features (Lee, Chen & Jiang, 1993 ;Jiang, Lee & Chen, 1994 ;Goldman-Levkovitz, Rimon & Rimon, 1995 ;Heu, Kim, Cho, Godber & Pyeun, 1997) and for their ability to degrade muscle proteins (Jiang, Wang & Chen, 1992 ;Aoki & Ueno, 1997 ;Aranishi, Ogata, Hara, Osatomi & Ishihara, 1998). It would be expected that the respective action of each protease is possibly affected by the other proteases.…”

Section: Introductionmentioning

confidence: 99%

Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.)

et al. 2004

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The effects of a milli(m)-calpain isolated from the white muscle of sea bass (Dicentrarchus labrax L) and commercial cathepsins B, D and L, used in combination on the myofibrillar and sarcoplasmic proteins were examined. Protein digestion was first performed by the endogenous m-calpain, during 2 h before the addition of a mixture of cathepsins B, D and L and a further incubation up to 22 h. Calpain degraded a 27 kDa sarcoplasmic component as well as myosin heavy chain, α-actinin, desmin and a 32 kDa component from the myofibrillar fraction. A 97 kDa component and the assumed creatine kinase-aldolase doublet were degraded during the incubation of sarcoplasmic proteins with the cathepsin mixture while, among the myofibrillar proteins, myosin, actin, tropomyosin, and the 22 kDa component were digested by the same enzymatic preparation. Myofibril-bound α-actinin and tropomyosin were released into the soluble fraction by m-calpain and the cathepsins mixture. Some smaller fragments were also produced. This appears to be the result of the cumulative action of each protease, as already investigated in our previous studies, except for the degradation of the sarcoplasmic 97 kDa component. It was only degraded if the cathepsins were mixed; this indicates that the three cathepsins functioned synergistically on muscle proteins. No difference in the proteolytic effect of cathepsins was observed, whether calpain was acting first or not. This work showed that calpain did not modify any muscle protein prior to later hydrolysis by the catheptic proteinases.

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Purification properties and specificity of cathepsin D from Cyprinus carpio

Cited by 14 publications

References 9 publications

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Partial characterization and activity distribution of proteases along the intestine of grass carp, Ctenopharyngodon idella (Val.)

Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.)

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