Plasmin Activity in Milk

Korycha-Dahl, M.; Dumas, Bruno; Chêne, N.; Martal, J.

doi:10.3168/jds.s0022-0302(83)81848-7

Cited by 169 publications

(120 citation statements)

References 16 publications

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“…Peptides having termini that pass a comparison to an enzymatic specificity have their abundances added to the sum of the respective enzyme. Proteases known to be present in milk include plasmin (48), trypsin (49,50), elastase (50), cathepsin-D (51), and thrombin (39). In addition, undefined carboxy/amino peptidases have been proposed to act in milk (20).…”

Section: Nano-lc Mass Spectrometry Analysis Of Endogenous Peptides Inmentioning

confidence: 99%

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Guerrero

Dallas

Contreras

et al. 2014

Molecular & Cellular Proteomics

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An extensive mass spectrometry analysis of the human milk peptidome has revealed almost 700 endogenous peptides from 30 different proteins. Two in-house computational tools were created and used to visualize and interpret the data through both alignment of the peptide quasi-molecular ion intensities and estimation of the differential enzyme participation. These results reveal that the endogenous proteolytic activity in the mammary gland is remarkably specific and well conserved. Certain proteins-not necessarily the most abundant ones-are digested by the proteases present in milk, yielding endogenous peptides from selected regions. Our results strongly suggest that factors such as the presence of specific proteases, the position and concentration of cleavage sites, and, more important, the intrinsic disorder of segments of the protein drive this proteolytic specificity in the mammary gland. As a consequence of this selective hydrolysis, proteins that typically need to be cleaved at specific positions in order to exert their activity are properly digested, and bioactive peptides encoded in certain protein sequences are released. Proteins that must remain intact in order to maintain their activity in the mammary gland or in the neonatal gastrointestinal tract are unaffected by the hydrolytic environment present in milk. These results provide insight into the intrinsic structural mechanisms that facilitate the selectivity of the endogenous milk protease activity and might be useful to those studying the peptidomes of other biofluids. Molecular &

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Section: Nano-lc Mass Spectrometry Analysis Of Endogenous Peptides Inmentioning

confidence: 99%

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Guerrero

Dallas

Contreras

et al. 2014

Molecular & Cellular Proteomics

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“…The possible existence of smail quantities of the whey Plg-activator (Korycka-Dahl et al, 1983) in our casein and our fraction (FZ) should not be excluded. Manji and Kakuda (1986) have shown that the enzymatic preparation obtained by chromatography of casein on LysineSepharose consists of 90% Pig and 10% Plm, indicating the possibility of selfactivation.…”

Section: Purification Of Map and Comparisons With Plgmentioning

confidence: 88%

Purification of bovine milk alkaline proteinase and comparison with purified bovine blood plasminogen or plasmin

Humbert

Berbar

Godbillon³

et al. 1990

Lait

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Summary -The bovine blood plasminogen (Plg) has been purified by affinity chromatography on Lysine-Sepharose. An electrophoresis pattern revealed sorne minor contaminant bands. The possibilities of contamination and activation of Pig have been examined; the Iikely causes of the heterogeneousness are: 1) an in vivo activation just before or during slaughter of the animais; 2) a partial activation during purification; 3) a self-activation or a self-hydrolyse which is a characteristic of proteinases or 4) a contamination of the chromatography column.The milk alkaline proteinase was purified by affinity chromatographies on Lysine-Sepharose and an immunoadsorbant (rabbit anti-bovine plasminogen serum) from whole casein and on enzymeenriched fraction. The purified fractions were partially heterogeneous and presented sorne minor components which are plasmin-chains. This sustains the assumption that self-activation or activation caused by traces of a whey activator in the whole casein occur. Blood and milk purified fractions were compared (electrophoresis, double-immunodiffusion, glycoprotein staining). This paper presents a nover method to purify the milk alkaline proteinase and to confirm the similarities between blood-and milk proteinase. milk alkaline proteinase 1 blood plasminogen or plasmin 1 purification 1 affinity chromategraphy 1 immunological reaction Résumé -Purification de la protéase alcaline du lait et comparaison avec la plasmine ou le plasminogène sanguins bovins purifiés. phy on Lysine-Sepharose will be described. Milk alkaline proteinase was also purified by affinity chromatography on immunoadsorbant using an antiplasminogen serum. Finally the products obtained by these purifications will be compared. Figure 1 depicts the experimental

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“…Segundo KORYCKA-DAHL et al (1983), a qualidade do leite e dos produtos lácteos pode ser influenciada por enzimas proteolíticas, como a plasmina. GASSEM e FRANK (1990), em estudo sobre o efeito da degradação da proteína do leite nas propriedades físico-químicas do iogurte, concluíram que proteases microbianas e a atividade da plasmina podem afetar a qualidade do produto.…”

Section: Proteasesunclassified

Avaliação do iogurte produzido com leite contendo diferentes níveis de células somáticas.

Fernandes¹,

Oliveira²

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Plasmin Activity in Milk

Cited by 169 publications

References 16 publications

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Purification of bovine milk alkaline proteinase and comparison with purified bovine blood plasminogen or plasmin

Avaliação do iogurte produzido com leite contendo diferentes níveis de células somáticas.

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