Cathepsin D

Fusek, Martin

doi:10.1016/b978-0-12-382219-2.00008-9

Cited by 10 publications

(14 citation statements)

References 128 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: 83%

“…; Fusek et al . ). The molecular weight of pepsin reported in the present study was similar to that reported by Bohak (); Fox et al .…”

Section: Resultsmentioning

confidence: 97%

“…Similar responses for cathepsin D have been reported by Fusek et al . () and Barrett (), while for pepsin pH optima for different substrates has been reported in the range of 1.6–1.8 by pepsin of sheep, ox and pig origin (Fox et al . ).…”

Section: Resultsmentioning

confidence: 99%

“…Cathepsin D from other sources have been reported to comprise of two chains (heavy and light), linked together by disulfide bonds (Fusek et al . ) and there is a distinct heterogeneity in the size of individual chains depending on the source (Huang et al . ; Goldman‐Levkovitz et al .…”

Section: Resultsmentioning

confidence: 99%

“…As cathepsin D has been reported to possess N‐linked glycosylation (Fusek et al . ), that might confer stability to the molecule at higher pH.…”

Section: Resultsmentioning

confidence: 99%

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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: 83%

“…; Fusek et al . ). The molecular weight of pepsin reported in the present study was similar to that reported by Bohak (); Fox et al .…”

Section: Resultsmentioning

confidence: 97%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…As cathepsin D has been reported to possess N‐linked glycosylation (Fusek et al . ), that might confer stability to the molecule at higher pH.…”

Section: Resultsmentioning

confidence: 99%

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Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Jamdar

Harikumar

2016

Journal of Food Biochemistry

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Trace levels of the CHO host cell protease cathepsin D caused particle formation in a monoclonal antibody product

Bee¹,

Liu²,

Johnson³

et al. 2015

Biotechnol Progress

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Chinese hamster ovary (CHO) cells are often used to produce therapeutic monoclonal antibodies (mAbs). CHO cells express many host cell proteins (HCPs) required for their growth. Interactions of HCPs with mAbs can sometimes result in co-purification of trace levels of 'hitchhiker' HCPs during the manufacturing process. Purified mAb-1 product produced in early stages of process optimization had high HCP levels. In addition, these lots formed delayed-onset particles containing mAb-1 and its heavy chain C-terminal fragments. Studies were performed to determine the cause of the observed particle formation and to optimize the purification for improved HCP clearance. Protease activity and inhibitor stability studies confirmed that an aspartyl protease was responsible for fragmentation of mAb-1 resulting in particle formation. An affinity resin was used to selectively capture aspartyl proteases from the mAb-1 product. Mass spectrometry identified the captured aspartyl protease as CHO cathepsin D. A wash step at high pH with salt and caprylate was implemented during the protein A affinity step to disrupt the HCP-mAb interactions and improve HCP clearance. The product at the end of purification using the optimized process had very low HCP levels, did not contain detectable protease activity, and did not form particles. Spiking of CHO cathepsin D back into mAb-1 product from the optimized process confirmed that it was the cause of the particle formation. This work demonstrated that process optimization focused on removal of HCPs was successful in eliminating particle formation in the final mAb-1 product.

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Design, synthesis, biological evaluation and molecular docking study based on novel fused pyrazolothiazole scaffold

et al. 2020

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Cathepsin D

Cited by 10 publications

References 128 publications

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Purification, Identification and Characterization of Aspartic Proteases of Chicken Intestine

Trace levels of the CHO host cell protease cathepsin D caused particle formation in a monoclonal antibody product

Design, synthesis, biological evaluation and molecular docking study based on novel fused pyrazolothiazole scaffold

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