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Bovine hyaluronidase

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Bovine hyaluronidase is an enzyme derived from bovine sources. It functions to catalyze the hydrolysis of hyaluronic acid, a component of the extracellular matrix.

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Lab products found in correlation

Trypsin, by Merck Group (2 mentions) 6 well culture plate, by Corning (1 mentions) Dextran sulfate, by Merck Group (1 mentions) Heparin, by Merck Group (1 mentions) Hyaluronidase from streptomyces hyalurolyticus, by Merck Group (1 mentions) Stains all, by Merck Group (1 mentions) Chondroitin sulfate b, by Merck Group (1 mentions) S4800 feg, by Hitachi (1 mentions) Streptavidin hrp, by Vector Laboratories (1 mentions) Dab kit, by Vector Laboratories (1 mentions) Anti mouse hrp, by Thermo Fisher Scientific (1 mentions) Anti mouse cy5, by Thermo Fisher Scientific (1 mentions) Streptavidin pe, by Vector Laboratories (1 mentions) Observer 2, by Zeiss (1 mentions) S 3400n 2, by Hitachi (1 mentions) Glutaraldehyde, by Merck Group (1 mentions) Protease inhibitor, by Merck Group (1 mentions) Maleimide peg nhs, by Nanocs (1 mentions) N hydroxysulfosuccinimide sulfo nhs, by Thermo Fisher Scientific (1 mentions) O phenylenediamine, by Thermo Fisher Scientific (1 mentions)

13 protocols using bovine hyaluronidase

1

Cumulus Dispersion for ICSI

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Oocytes used for directly ICSI were treated with bovine hyaluronidase (Sigma-Aldrich; Merck KGaA) for dispersing the cumulus cells after 39~40 h of trigger. And the MII oocytes undergo the ICSI insemination.
Jiang Y., Yuan J.C., Song G., Zhang X.H., Miao S.B, & Wu X.H. (2023). Comparing the pregnancy outcomes of Re‑ICSI and ICSI embryos in fresh ET and FET cycles. Biomedical Reports, 19(4), 66.
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2

In Vivo Transfection of Plasmid pMGF

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Expression plasmid pMGF was in vivo transfected using electroporation. Briefly, animals were first anesthetized, and then the TA muscle was injected with 20 μl of filter-sterilized bovine hyaluronidase (0.4 U/μl in 0.9% m/v saline; Sigma-Aldrich, United States). Two hours later, 25 μg of filter-sterilized pMGF plasmid (1 μg/μl in 0.45% m/v saline) was injected. The use of both hyaluronidase (McMahon et al., 2001 (link)) and 0.45% m/v saline (Lee et al., 2002 (link)) maximizes electroporation efficiency. Immediately after pMGF injection, platinum tweezertrodes (5 mm diameter, BTX, United States) were placed longitudinally relative to the TA muscle, and electroporation was performed by applying 10 square-wave pulses (ECM830, BTX, United States) of 20 ms and 175 V/cm at a frequency of 1 Hz (McMahon et al., 2001 (link)). The contralateral TA muscle was electroporated with mock vector (pcDNA 3.1) in the same manner and served as a negative control. Specific transfection of TA muscle by electroporation and the expression of 6-HIS tagged MGF peptide were demonstrated by in vivo imaging and Western blotting, respectively (Figure 1).
Sun K.T., Cheung K.K., Au S.W., Yeung S.S, & Yeung E.W. (2018). Overexpression of Mechano-Growth Factor Modulates Inflammatory Cytokine Expression and Macrophage Resolution in Skeletal Muscle Injury. Frontiers in Physiology, 9, 999.
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3

Hyaluronidase Treatment Effects on Tissue Constructs

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After a culture period of 7–11 weeks (8.8 ± 1.6weeks), three constructs per patient were treated with either culture medium containing 600U/mL bovine hyaluronidase (Sigma Aldrich, St. Louis, Mo) or a mock treatment of culture medium without the enzyme for 24 hours at 37°C with 5% carbon dioxide. After treatment, the constructs were rinsed in PBS and transferred into 6-well culture plate (Corning, Inc., Corning, NY) containing culture medium and cultured for another 3, 6, or 9 weeks. At the end of the culture period, constructs were harvested, weighed, and evaluated.
Watson D., Reuther M.S., Wong V.W., Sah R.L., Masuda K, & Briggs K.K. (2016). Effect of Hyaluronidase on Tissue Engineered Human Septal Cartilage. The Laryngoscope, 126(9), 1984-1989.
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4

Hyaluronidase Substrate Specificity Assay

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Five micrograms of HA of different sizes (high, medium and low molecular weight, which correspond to > 950 kDa, 75–350 kDa and 15–40 kDa, respectively, RD Systems, Minneapolis, MN) were incubated for 1 h at 37°C with SGE (equivalent of 1 SG pair) or LuloHya (10 nM). Other commercial hyaluronidases were included as controls: bovine hyaluronidase (Sigma) and hyaluronidase from Streptomyces hyalurolyticus (Sigma), both at 1 Unit per reaction. Samples were run on a 1.2% agarose gel for 30 min at 20 V followed by 2 h 30 min at 40 V. Agarose gels were stained with 0.05% Stains-all (Sigma).
For hyaluronidase activity specificity, other glycosaminoglycan components of the extracellular matrix were also tested, including chondroitin sulfate B, dextran sulfate and heparin (5 μg/sample, Sigma).
Martin-Martin I., Chagas A.C., Guimaraes-Costa A.B., Amo L., Oliveira F., Moore I.N., DeSouza-Vieira T.S., Sanchez E.E., Suntravat M., Valenzuela J.G., Ribeiro J.M, & Calvo E. (2018). Immunity to LuloHya and Lundep, the salivary spreading factors from Lutzomyia longipalpis, protects against Leishmania major infection. PLoS Pathogens, 14(5), e1007006.
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5

Proteoglycan Extraction from Articular Cartilage

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Following the method of Segawa and Takiguchi [32 (link)], proteoglycans were extracted from articular cartilage specimens in 100 mM Soerensen’s phosphate buffer (pH 7.2) containing 1mg/ml bovine hyaluronidase (type I-S Sigma, St Louis, MO, USA) and 1mg/ml trypsin (type I, Sigma, St Louis, MO, USA) and 0.5% sodium azide for 3 days at 37°C. The solution was renewed every 24 h. Specimens were then fixed with a 2.5% gluteraldehyde (in PBS, 2.6 mM NaH2PO4, 3 mM Na2HPO4, 155 mM NaCl, 0.01% NaN3 w/v, pH 7.2) for 2.5 h at room temperature. Next, they were vortexed three times in ultrapure water and dehydrated in an ascending ethanol series up to 100%). After critical point drying, samples were sputter-coated with 3–5 nm of platinum and examined by SEM (Hitachi S-4800 FEG) operated at 1.5–5 kV accelerating voltage. Areas corresponding to joint surface were selected for imaging, choosing flat, uniform parts, and avoiding any macroscopic defects as well as the territorial and pericellular envelope of surface chondrocytes.
Gottardi R., Hansen U., Raiteri R., Loparic M., Düggelin M., Mathys D., Friederich N.F., Bruckner P, & Stolz M. (2016). Supramolecular Organization of Collagen Fibrils in Healthy and Osteoarthritic Human Knee and Hip Joint Cartilage. PLoS ONE, 11(10), e0163552.
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6

Visualization of Hyaluronan and Staphylococcal Toxin in Tumor Sections

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Prior to incubation with bHs-ST in vitro, sections of PANC-1 tumors were de-paraffinized and rehydrated. Uninduced and induced χ8768-bHs (108 CFU), PBS or bovine hyaluronidase (Sigma) were incubated on tissue sections overnight in a humidified 37°C incubator. Following treatment, specimens were incubated with a biotinylated HA binding protein (HABP, Sigma) at 5 μg/mL final concentration for 2 hours at 37°C. Slides were then washed, incubated with streptavidin-HRP at RT for 1 hr and visualized with a DAB kit (Vectastain). H&E and Masson’s Tricrhome were used for staining. PANC-1 tumor sections, skin and decalcified joints from NSG mice treated intravenously with χ8768-bHs (uninduced and induced). Sections were de-paraffinized and rehydrated and stained overnight with 2.5 μg/mL HABP, 1:100 anti-ST antibody (Santa Cruz, sc-52223), 1:100 anti-pan-cytokeratin (AE1/AE3) or according to H&E and Masson’s Trichrome protocols used by the Pathology Research Services Core (City of Hope). Streptavidin-PE (Vector), anti-mouse-Cy5 (Invitrogen), or anti-mouse-HRP 1:250 were then used to visualize HA, ST or pan-cytokeratin by brightfield or fluorescence microscopy (Zeiss Observer II), in addition to DAPI for visualizing nuclei during fluorescence imaging. Tiling was performed at 5X or 10X, while higher resolution images for ST, HA and DAPI were done at 100X (oil).
Ebelt N.D., Zuniga E., Passi K.B., Sobocinski L.J, & Manuel E.R. (2019). Hyaluronidase-Expressing Salmonella Effectively Targets Tumor-Associated Hyaluronic Acid in Pancreatic Ductal Adenocarcinoma. Molecular cancer therapeutics, 19(2), 706-716.
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7

Measuring Bone Resorption Biomarker in Dogs

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The bone resorption biomarker helical peptide (HP) in dog urine was measured using an enzyme-linked immunosorbent assay followed by normalization to creatinine level determined from the same sample.10 For synovial fluid, samples were pretreated with bovine hyaluronidase (Sigma, St Louis, Missouri, USA; 1 unit per 0.2 mL synovial fluid) at 37°C overnight was performed prior to quantification.
Ma B., Wesolowski G., Luo B., Lifsted T., Wessner K., Adamson G., Glantschnig H, & Lubbers L.S. (2019). Suppression of cathepsin K biomarker in synovial fluid as a free-drug–driven process. Journal of Circulating Biomarkers, 8, 1849454418821819.
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8

Collagen Structure Analysis of CEP Samples

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SEM detected the collagen structures of CEP samples, as described previously21 . Briefly, proteoglycans were extracted from CEP samples in 100 mM Soerensen’s phosphate buffer (pH 7.2) (Sigma-Aldrich) containing 1 mg/mL trypsin (Sigma-Aldrich), 1 mg/mL bovine hyaluronidase (Sigma-Aldrich), protease inhibitors (Sigma-Aldrich) and 0.01% NaN3 (Sigma-Aldrich) at 37 °C for 3 days. The samples were fixed with 2.5% glutaraldehyde (Sigma-Aldrich) in PBS and dehydrated in a graded ethanol series. After point drying, the CEP samples were sputter-coated with 3–5 nm platinum and examined with an SEM (S-3400N II-Hitachi, Japan) at 1.5–5 kV accelerating voltage.
Liu M.H., Sun C., Yao Y., Fan X., Liu H., Cui Y.H., Bian X.W., Huang B, & Zhou Y. (2016). Matrix stiffness promotes cartilage endplate chondrocyte calcification in disc degeneration via miR-20a targeting ANKH expression. Scientific Reports, 6, 25401.
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9

Prostate Cancer Cell Targeting Nanoparticle Formulation

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Recombinant human hyaluronidase, PH20 (rHuPH20) in pH=6.5, 10 mM sodium phosphate, 150 mM NaCl buffer was obtained from Halozyme, Inc.. Poly(D,L-lactide-co-glycolide) with PLA:PGA ratio of 50:50 (Mw = 47.5 kDa, inherent viscosity = 0.66 dL/g) was purchased from DURECT Corporation. PC3 prostate cancer cell line was purchased from ATCC Inc. 1,2-dimyristoyl-sn-glycero-3-phospho-ethanolamine-N-(lissamine rhodamine B sulfonyl) (ammonium salt) (Rhod-PE) was acquired from Avanti Polar Lipids Inc. Long linker, succinimidyl-[(N-maleimidopropionamido)-polyethyleneglycol] ester (NHS-PEG-Maleimide, Mw = 3400) was purchased from NANOCS, whereas short linker, succinimidyl-[(N-maleimidopropionamido)-diethyleneglycol] ester (NHS-PEG2-Maleimide, Mw = 425), o-Phenylene-diamine (OPD), 1,1'-Dioctadecyl-3,3,3',3'-Tetramethylindodicarbocyanine Perchlorate (DiD), horseradish peroxidase conjugated streptavidin (HRP-streptavidin), 2-Iminothiolane•HCl (Traut's Reagent), N-hydroxysulfosuccinimide (Sulfo-NHS), 1-ethyl-3-(3-dimethylamin-opropyl) carbidodiimide (EDC) and (biotinyl)hydrazide (Biotin hydrazide) were purchased from ThermoFisher Scientific. Bovine hyaluronidase was purchased form Sigma-Aldrich. Additional salts, solvents and buffers were purchased from Fisher Scientific.
Zhou H., Fan Z., Lemons P.K, & Cheng H. (2016). A Facile Approach to Functionalize Cell Membrane-Coated Nanoparticles. Theranostics, 6(7), 1012-1022.
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10

Spectrophotometric Hyaluronidase Activity Assay

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Hyaluronidase activity was evaluated spectrophotometrically by measuring the amount of N-acetylglucosamine formed from sodium hyaluronate [52 (link)]. The tested compound and reference control were prepared in concentrations ranging from 0.1 to 100 µg/mL for the analysis. Fifty microliters of bovine hyaluronidase (7900 units mL−1, (Sigma, St. Louis, MO, USA) dissolved in 0.1 M acetate buffer (pH = 3.5) was mixed with 100 µL of a designated concentration of the compound dissolved in 5% DMSO and then incubated in a water bath at 37 °C for 20 min. The control group was treated with 100 µL of 5% DMSO instead of the sample. The optical density of the reaction mixture was measured at 585 nm by spectrophotometry.
El-Nashar H.A., El-labbad E.M., Al-Azzawi M.A, & Ashmawy N.S. (2022). A New Xanthone Glycoside from Mangifera indica L.: Physicochemical Properties and In Vitro Anti-Skin Aging Activities. Molecules, 27(9), 2609.
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