Proteolytic activity of bovine lactoferrin

Massucci, Maria; Giansanti, Francesco; Nino, Giovanna Di; Turacchio, Manola; Giardi, Maria Federica; Botti, Dario; Ippoliti, Rodolfo; Giulio, Beatrice De; Siciliano, Rosa Anna; Donnarumma, Giovanna; Valenti, Piera; Bocedi, Alessio; Polticelli, Fabio; Ascenzi, Paolo; Antonini, Giovanni

doi:10.1007/s10534-004-5667-x

Cited by 2 publications

(2 citation statements)

References 14 publications

(23 reference statements)

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“…Lactoferrin at pH 2.6, 3.5, and 7.0 all appeared as intense bands (lanes 3, 4, and 5, respectively) around 70 kDa as expected of its molecular weight (~72.5 to 77.1; Castellino et al, 1970). Three bands with the molecular weight around 45, 36, and 28 kDa, respectively, were observed and could be the breakdown products of lactoferrin under reducing conditions (Massucci et al, 2004). Mixing saliva and lactoferrin at all pH values resulted in turbid samples, which were separated into supernatant and pellet after centrifugation.…”

Section: Identifying the Interactions Between β-Lg Or Lactoferrin And Salivary Proteins Using Sds-pagementioning

confidence: 63%

Roles of charge interactions on astringency of whey proteins at low pH

Vardhanabhuti

Kelly

Luck

et al. 2010

Journal of Dairy Science

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Whey proteins are a major ingredient in sports drink and functional beverages. At low pH, whey proteins are astringent, which may be undesirable in some applications. Understanding the astringency mechanism of whey proteins at low pH could lead to developing ways to minimize the astringency. This study compared the astringency of beta-lactoglobulin (beta-LG) at low pH with phosphate buffer controls having the same amount of phosphate and at similar pH. Results showed that beta-LG samples were more astringent than phosphate buffers, indicating that astringency was not caused by acid alone and that proteins contribute to astringency. When comparing among various whey protein isolates (WPI) and lactoferrin at pH 3.5, 4.5, and 7.0, lactoferrin was astringent at pH 7.0 where no acid was added. In contrast, astringency of all WPI decreased at pH 7.0. This can be explained by lactoferrin remaining positively charged at pH 7.0 and able to interact with negatively charged saliva proteins, whereas the negatively charged WPI would not interact. Charge interactions were further supported by beta-LG or lactoferrin and salivary proteins precipitating when mixed at conditions where beta-LG, lactoferrin, or saliva themselves did not precipitate. It can be concluded that interactions between positively charged whey proteins and salivary proteins play a role in astringency of proteins at low pH.

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Section: Identifying the Interactions Between β-Lg Or Lactoferrin And Salivary Proteins Using Sds-pagementioning

confidence: 63%

Roles of charge interactions on astringency of whey proteins at low pH

Vardhanabhuti

Kelly

Luck

et al. 2010

Journal of Dairy Science

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“…The question of what type of a protein secondary structure is susceptible to proteolysis still remains controversial. Thus, the long-established opinion that cleavages are possible only in loops was recently challenged by findings that registered the occurrence of cleavage sites in ␣-helices [16,33] and ␤-sheets [34,35]. To clarify this issue, we analyzed the secondary-structure context of 4576 unique cleavage positions (fewer than the total number of proteolytic events, as more than one protease could cleave the same site) taken from CutDB.…”

Section: Secondary-structure Context Of Proteolytic Eventsmentioning

confidence: 99%

Sequence‐derived structural features driving proteolytic processing

et al. 2013

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Proteolytic signaling, or regulated proteolysis, is an essential part of many important pathways such as Notch, Wnt, and Hedgehog. How the structure of the cleaved substrate regions influences the efficacy of proteolytic processing remains underexplored. Here, we analyzed the relative importance in proteolysis of various structural features derived from substrate sequences using a dataset of more than five thousand experimentally verified proteolytic events captured in CutDB. Accessibility to the solvent was recognized as an essential property of a proteolytically processed polypeptide chain. Proteolytic events were found nearly uniformly distributed among three types of secondary structure, although with some enrichment in loops. Cleavages in α-helices were found to be relatively abundant in regions apparently prone to unfolding, while cleavages in β-structures tended to be located at the periphery of β-sheets. Application of the same statistical procedures to proteolytic events divided into separate sets according to the catalytic classes of proteases proved consistency of the results and confirmed that the structural mechanisms of proteolysis are universal. The estimated prediction power of sequence-derived structural features, which turned out to be sufficiently high, presents a rationale for their use in bioinformatic prediction of proteolytic events.

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Proteolytic activity of bovine lactoferrin

Cited by 2 publications

References 14 publications

Roles of charge interactions on astringency of whey proteins at low pH

Roles of charge interactions on astringency of whey proteins at low pH

Sequence‐derived structural features driving proteolytic processing

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