Matches in SemOpenAlex for { <https://semopenalex.org/work/W4289965385> ?p ?o ?g. }
Showing items 1 to 55 of
55
with 100 items per page.
- W4289965385 endingPage "9" @default.
- W4289965385 startingPage "105" @default.
- W4289965385 abstract "Preparations of acidic gamma-amylase, which cleaved glycogen and maltose, were isolated from human and rabbit brain tissues. The specific activity of the gamma-amylase preparations from human brain was approximately twice higher than the activity of the enzyme from rabbit brain. In degradation of glycogen gamma-amylases from human and rabbit brain had the pH optima at pH 4.9 and 4.6 and with maltose as a substrate- at pH 4.3 and 4.1, respectively. gamma-Amylases from both sources possessed the high stability in presence of monovalent cations. K+ distinctly increased the cleavage of glycogen by gamma-amylase from human and rabbit brain. alpha, alpha-Trehalose and alpha-menthyl glucoside proved to be inhibitors of the glucoamylase activity of the enzymes from both sources. Km values of the gamma-amylases for glycogen were equal to 19.3 mM 19.8 and for maltose -5.54 mM and 5.78 mM, respectively. The data obtained suggest that acidic gamma-amylases from human and rabbit brain are similar to acidic gamma-amylases from other sources." @default.
- W4289965385 created "2022-08-06" @default.
- W4289965385 creator A5058459226 @default.
- W4289965385 creator A5065137752 @default.
- W4289965385 date "1977-01-01" @default.
- W4289965385 modified "2023-09-24" @default.
- W4289965385 title "[Acid gamma-amylase of rabbit and human brain]." @default.
- W4289965385 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16385" @default.
- W4289965385 hasPublicationYear "1977" @default.
- W4289965385 type Work @default.
- W4289965385 citedByCount "0" @default.
- W4289965385 crossrefType "journal-article" @default.
- W4289965385 hasAuthorship W4289965385A5058459226 @default.
- W4289965385 hasAuthorship W4289965385A5065137752 @default.
- W4289965385 hasConcept C169760540 @default.
- W4289965385 hasConcept C170835558 @default.
- W4289965385 hasConcept C173959671 @default.
- W4289965385 hasConcept C181199279 @default.
- W4289965385 hasConcept C185592680 @default.
- W4289965385 hasConcept C2777499176 @default.
- W4289965385 hasConcept C2777670902 @default.
- W4289965385 hasConcept C2778197599 @default.
- W4289965385 hasConcept C43617362 @default.
- W4289965385 hasConcept C55493867 @default.
- W4289965385 hasConcept C86803240 @default.
- W4289965385 hasConceptScore W4289965385C169760540 @default.
- W4289965385 hasConceptScore W4289965385C170835558 @default.
- W4289965385 hasConceptScore W4289965385C173959671 @default.
- W4289965385 hasConceptScore W4289965385C181199279 @default.
- W4289965385 hasConceptScore W4289965385C185592680 @default.
- W4289965385 hasConceptScore W4289965385C2777499176 @default.
- W4289965385 hasConceptScore W4289965385C2777670902 @default.
- W4289965385 hasConceptScore W4289965385C2778197599 @default.
- W4289965385 hasConceptScore W4289965385C43617362 @default.
- W4289965385 hasConceptScore W4289965385C55493867 @default.
- W4289965385 hasConceptScore W4289965385C86803240 @default.
- W4289965385 hasIssue "1" @default.
- W4289965385 hasLocation W42899653851 @default.
- W4289965385 hasOpenAccess W4289965385 @default.
- W4289965385 hasPrimaryLocation W42899653851 @default.
- W4289965385 hasRelatedWork W1551625927 @default.
- W4289965385 hasRelatedWork W2000491116 @default.
- W4289965385 hasRelatedWork W2057379811 @default.
- W4289965385 hasRelatedWork W2064273560 @default.
- W4289965385 hasRelatedWork W2172218933 @default.
- W4289965385 hasRelatedWork W2414121143 @default.
- W4289965385 hasRelatedWork W2800040682 @default.
- W4289965385 hasRelatedWork W3126853549 @default.
- W4289965385 hasRelatedWork W3186707594 @default.
- W4289965385 hasRelatedWork W2166758582 @default.
- W4289965385 isParatext "false" @default.
- W4289965385 isRetracted "false" @default.
- W4289965385 workType "article" @default.