scholarly journals PENENTUAN UMUR SIMPAN OTAK-OTAK IKAN UMKM BUNGA MAWAR DENGAN METODE EXTENDED STORAGE STUDIES (ESS)

2021 ◽  
Vol 2 (2) ◽  
pp. 101
Author(s):  
Asriani Asriani ◽  
Niken Dharmayanti ◽  
Henny Budi Purnamasari ◽  
Yudi Prasetyo Handoko ◽  
Nofi Sulistiyo Rini ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
G Protein ◽  
Storage Studies

Otak-otak ikan merupakan salah satu produk diversifikasi hasil perikanan yang sudah lama dikenal dan disukai oleh masyarakat di Indonesia. Otak-otak ikan yang bersifat semi basah biasanya memiliki umur simpan yang singkat sehingga penentuan informasi umur simpan produk menjadi penting. Tujuan penelitian ini adalah untuk mengetahui karakteristik mutu bahan baku dan produk akhir, kandungan nilai gizi, serta umur simpan dari otak-otak ikan yang diproduksi UMKM Bunga Mawar dengan metode Extended Storage Studies (ESS). Mutu otak-otak ikan UMKM Bunga Mawar sesuai dengan SNI (7757:2013). Nilai sensori produk otak-otak ikan adalah 9. Kadar air 50,19%, kadar abu 1,22%, Protein 7%, Lemak 2,95%. Karbohidrat 38,64%, ALT 2 x 10 3 Kol/g. E.Coli < 3 APM / 25g, Salmonella Negatif, dan S Staphylococcus aureus 57 kol/g. Nilai gizi otak-otak ikan UMKM Bunga Mawar pertakaran saji 50 g antara lain energi total 100 kkal, energi dari lemak 9 kkal dengan lemak 1 g, protein 7 g, karbohidrat 15 g, persentase AKG berdasarkan kebutuhan umum 2.150 kkal antara lain lemak 2%, protein 7%, karbohidrat 9%. Umur simpan otak-otak ikan UMKM Bunga Mawar yang dibungkus menggunakan plastik PE tanpa divakum pada suhu 5°C adalah 6 hari dan pada suhu 30°C adalah 4 hari.

scholarly journals Molecular insights into mechanisms of GPCR hijacking by Staphylococcus aureus

2021 ◽  
Vol 118 (42) ◽  
pp. e2108856118
Author(s):  
Claire M. Grison ◽  
Paul Lambey ◽  
Sylvain Jeannot ◽  
Elise Del Nero ◽  
Simon Fontanel ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Staphylococcus Aureus ◽  
G Protein ◽  
Protein Complexes ◽  
Native Mass Spectrometry ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Exchange Mass Spectrometry ◽  
Toxin Binding ◽  
And Function

Atypical chemokine receptor 1 (ACKR1) is a G protein–coupled receptor (GPCR) targeted by Staphylococcus aureus bicomponent pore-forming leukotoxins to promote bacterial growth and immune evasion. Here, we have developed an integrative molecular pharmacology and structural biology approach in order to characterize the effect of leukotoxins HlgA and HlgB on ACKR1 structure and function. Interestingly, using cell-based assays and native mass spectrometry, we found that both components HlgA and HlgB compete with endogenous chemokines through a direct binding with the extracellular domain of ACKR1. Unexpectedly, hydrogen/deuterium exchange mass spectrometry analysis revealed that toxin binding allosterically modulates the intracellular G protein–binding domain of the receptor, resulting in dissociation and/or changes in the architecture of ACKR1−Gαi1 protein complexes observed in living cells. Altogether, our study brings important molecular insights into the initial steps of leukotoxins targeting a host GPCR.

scholarly journals Mechanisms of GPCR hijacking by Staphylococcus aureus

2021 ◽  
Author(s):  
Claire M. Grison ◽  
Cédric Leyrat ◽  
Paul Lambey ◽  
Sylvain Jeannot ◽  
Elise Del Nero ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
G Protein ◽  
Protein Complexes ◽  
Native Mass Spectrometry ◽  
Molecular Pharmacology ◽  
Toxin Binding ◽  
Direct Binding ◽  
And Function ◽  
Hdx Ms ◽  
G Protein Coupled

SUMMARYAtypical chemokine receptor 1 (ACKR1) is a G protein-coupled receptor (GPCR) targeted by Staphylococcus aureus (SA) bi-component pore-forming leukotoxins to promote bacterial growth and immune evasion. Here we have developed an integrative molecular pharmacology and structural biology approach in order to characterize the effect of leukotoxins HlgA and HlgB on ACKR1 structure and function. Interestingly, we found that both components HlgA and HlgB compete with endogenous chemokines through a direct binding to ACKR1 captured by native mass spectrometry (MS). Unexpectedly, HDX-MS analysis revealed that toxin binding allosterically modulates the intracellular G protein-binding domain of the receptor, resulting in dissociation of ACKR1–G protein complexes in living cells. Altogether, our study brings important molecular insights into the initial steps of leukotoxins targeting a host GPCR. Our findings may open the way to develop antibiotics inhibiting host receptors binding, a mechanism of action less prone to resistance.

Formation and Structure of Casein Micelles in Lactating Mammary Tissue

1970 ◽  
Vol 28 ◽  
pp. 150-151
Author(s):  
Robert J. Carroll ◽  
Marvin P. Thompson ◽  
Harold M. Farrell
Keyword(s):  
Size Distribution ◽  
G Protein ◽  
Milk Proteins ◽  
Mammary Tissue ◽  
Colloidal System ◽  
Casein Micelles ◽  
The Stability

Milk is an unusually stable colloidal system; the stability of this system is due primarily to the formation of micelles by the major milk proteins, the caseins. Numerous models for the structure of casein micelles have been proposed; these models have been formulated on the basis of in vitro studies. Synthetic casein micelles (i.e., those formed by mixing the purified αsl- and k-caseins with Ca2+ in appropriate ratios) are dissimilar to those from freshly-drawn milks in (i) size distribution, (ii) ratio of Ca/P, and (iii) solvation (g. water/g. protein). Evidently, in vivo organization of the caseins into the micellar form occurs in-a manner which is not identical to the in vitro mode of formation.

Cytochemical Studies of Cell Wall Biosynthesis in Staphylococcus Aureus

1972 ◽  
Vol 30 ◽  
pp. 328-329
Author(s):  
Masaatsu Koike ◽  
Koichi Nakashima ◽  
Kyoko Iida
Keyword(s):  
Staphylococcus Aureus ◽  
Periodate Oxidation ◽  
Early Time ◽  
The Other ◽  
Penicillin G ◽  
Cell Wall Biosynthesis ◽  
Septal Wall ◽  
Peptidoglycan Biosynthesis ◽  
Gram Positive Bacteria ◽  
Cross Linkage

Penicillin exerts the activity to inhibit the peptide cross linkage between each polysaccharide backbone at the final stage of wall-peptidoglycan biosynthesis of bacteria. Morphologically, alterations of the septal wall and mesosome in gram-positive bacteria, which were occurred in early time after treatment with penicillin, have been observed. In this experiment, these alterations were cytochemically investigated by means of silver-methenamine staining after periodate oxidation, which is applied for detection of localization of wall mucopolysaccharide.Staphylococcus aureus strain 209P treated with 100 u/ml of penicillin G was divided into two aliquotes. One was fixed by Kellenberger-Ryter's OSO4 fixative at 30, 60 and 120 min after addition of the antibiotic, dehydrated through alcohol series, and embedded in Epon 812 (Specimen A). The other was fixed by 21 glutaraldehyde, dehydrated through glycolmethacrylate series and embedded in glycolmethacrylate mixture, according to Bernhard's method (Specimen B).

Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

1990 ◽  
Vol 48 (3) ◽  
pp. 578-579
Author(s):  
Margaret Hukee
Keyword(s):  
Staphylococcus Aureus ◽  
Teichoic Acid ◽  
Protein Labeling ◽  
Minimal Amount ◽  
Section Thickness ◽  
Double Labeling ◽  
Parallel Surfaces ◽  
Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

A compendium of G-protein–coupled receptors and cyclic nucleotide regulation of adipose tissue metabolism and energy expenditure

2020 ◽  
Vol 134 (5) ◽  
pp. 473-512 ◽  
Author(s):  
Ryan P. Ceddia ◽  
Sheila Collins
Keyword(s):  
Adipose Tissue ◽  
Energy Expenditure ◽  
Signaling Pathways ◽  
G Protein ◽  
Uncoupling Protein ◽  
Beige Adipocytes ◽  
Nucleotide Regulation ◽  
Ucp1 Expression ◽  
Thermogenic Adipocytes ◽  
G Protein Coupled

Abstract With the ever-increasing burden of obesity and Type 2 diabetes, it is generally acknowledged that there remains a need for developing new therapeutics. One potential mechanism to combat obesity is to raise energy expenditure via increasing the amount of uncoupled respiration from the mitochondria-rich brown and beige adipocytes. With the recent appreciation of thermogenic adipocytes in humans, much effort is being made to elucidate the signaling pathways that regulate the browning of adipose tissue. In this review, we focus on the ligand–receptor signaling pathways that influence the cyclic nucleotides, cAMP and cGMP, in adipocytes. We chose to focus on G-protein–coupled receptor (GPCR), guanylyl cyclase and phosphodiesterase regulation of adipocytes because they are the targets of a large proportion of all currently available therapeutics. Furthermore, there is a large overlap in their signaling pathways, as signaling events that raise cAMP or cGMP generally increase adipocyte lipolysis and cause changes that are commonly referred to as browning: increasing mitochondrial biogenesis, uncoupling protein 1 (UCP1) expression and respiration.

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