scholarly journals ELECTRON MICROSCOPY AND X-RAY SCANNING MICROANALYSIS OF NEEDLE BIOPSY MATERIAL FROM HUMAN LIVER

1962 ◽  
Vol 14 (3) ◽  
pp. 421-431 ◽  
Author(s):  
G. Yasuzumi
Keyword(s):  
Electron Microscopy ◽  
Needle Biopsy ◽  
Human Liver ◽  
Pancreatic Tumor ◽  
Biopsy Material ◽  
Cytoplasmic Matrix ◽  
X Ray ◽  
Iron Sample ◽  
Human Biopsy ◽  
Parenchymal Cells

A study has been made of the fine structure of hepatic parenchymal cells of human biopsy material in a case of pancreatic tumor with obstructive jaundice. Dense particles about 60 A in diameter have been found in the cytoplasm, which are considered to be ferritin molecules by electron microscopy. They are encountered throughout the cytoplasmic matrix and are often aggregated in electron-transparent areas, most of which are enclosed by an apparently single-layered membrane. Identification of the elemental iron has been pursued by the application of the x-ray scanning microanalyser which reveals a quantitative value within 1.0 per cent of the pure iron sample. The use of x-ray scanning microanalysis enables one to obtain accurate data from extremely small and precisely defined volumes of biological specimens.

scholarly journals Electron Microscopy, Electron Probe X-Ray Microanalysis and Microdiffraction of Biopsy Material from Human Liver

1969 ◽  
Vol 45 (6) ◽  
pp. 279-307 ◽  
Author(s):  
Gonpachiro Yasuzumi ◽  
Isako Tsubo ◽  
Kiyobumi Okada ◽  
Hitoshi Takahashi
Keyword(s):  
Electron Microscopy ◽  
Electron Probe ◽  
Human Liver ◽  
Biopsy Material ◽  
X Ray

scholarly journals Immunocytochemical localization of cytosol 5'-nucleotidase in chicken liver.

1988 ◽  
Vol 36 (8) ◽  
pp. 983-989 ◽  
Author(s):  
S Yokota ◽  
J Oka ◽  
H Ozasa ◽  
R Itoh
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Chicken Liver ◽  
Immunocytochemical Localization ◽  
Cell Organelles ◽  
Cytoplasmic Matrix ◽  
Tissue Sections ◽  
Fab Fragments ◽  
Parenchymal Cells ◽  
Immunoenzyme Technique

We investigated the localization of cytosol 5'-nucleotidase in chicken liver by use of a pre-embedding immunoenzyme technique. Cytosol 5'-nucleotidase was purified from chicken liver and a monospecific antibody to this enzyme was raised in a rabbit. Fab fragments of the antibody were conjugated with horseradish peroxidase. Tissue sections of the fixed chicken liver were incubated with the peroxidase-Fab fragments, followed by DAB reaction for peroxidase. By light microscopy, dark-brown staining was present in the cytoplasm of parenchymal cells, Kupffer cells, and endothelial cells. The latter two types of cells were stained more strongly than the former. By electron microscopy, reaction deposits were present in the cytoplasmic matrix but not in cell organelles, such as mitochondria, endoplasmic reticulum, and peroxisomes, or in nuclei. In control sections incubated with peroxidase-conjugated Fab fragments from non-immunized rabbit, no specific reaction was noted. The results indicate that cytosol 5'-nucleotidase is contained more in the sinus-lining cells and less in the parenchymal cells, and that the enzyme is present in the cytoplasmic matrix of these cells.

scholarly journals Scanning electron microscopy of hepatocyte cytoskeleton of human liver tissue taken by needle biopsy.

Kanzo ◽  
1987 ◽  
Vol 28 (9) ◽  
pp. 1259-1260
Author(s):  
Takeshi OKANOUE ◽  
Kazutomo KACHI ◽  
Yoshiharu OHTA ◽  
Masaharu OHTA ◽  
Hikoharu KANAOKA ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Liver Tissue ◽  
Needle Biopsy ◽  
Human Liver ◽  
Human Liver Tissue ◽  
Scanning Electron

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

Phase Transformations in Ti-7w/oMo-3w/oMe Alloy

1974 ◽  
Vol 32 ◽  
pp. 514-515
Author(s):  
S. Fujishiro
Keyword(s):  
Electron Microscopy ◽  
Mechanical Properties ◽  
Transmission Electron Microscopy ◽  
Tensile Strength ◽  
Mechanical Processing ◽  
Ray Method ◽  
X Ray ◽  
Transmission Electron ◽  
Water Quench ◽  
Alpha Beta

The mechanical properties of three titanium alloys (Ti-7Mo-3Al, Ti-7Mo- 3Cu and Ti-7Mo-3Ta) were evaluated as function of: 1) Solutionizing in the beta field and aging, 2) Thermal Mechanical Processing in the beta field and aging, 3) Solutionizing in the alpha + beta field and aging. The samples were isothermally aged in the temperature range 300° to 700*C for 4 to 24 hours, followed by a water quench. Transmission electron microscopy and X-ray method were used to identify the phase formed. All three alloys solutionized at 1050°C (beta field) transformed to martensitic alpha (alpha prime) upon being water quenched. Despite this heavily strained alpha prime, which is characterized by microtwins the tensile strength of the as-quenched alloys is relatively low and the elongation is as high as 30%.

Electron Microscopy of Cytoplasmic Contractile Proteins

1978 ◽  
Vol 36 (3) ◽  
pp. 606-614 ◽  
Author(s):  
T.D. Pollard ◽  
P. Maupin
Keyword(s):  
Electron Microscopy ◽  
Actin Filaments ◽  
Three Dimensional ◽  
Uranyl Acetate ◽  
Contractile Proteins ◽  
Dimensional Structure ◽  
X Ray Diffraction ◽  
Cytoplasmic Matrix ◽  
Computer Image Processing ◽  
Nonmuscle Cells

In this paper we review some of the contributions that electron microscopy has made to the analysis of actin and myosin from nonmuscle cells. We place particular emphasis upon the limitations of the ultrastructural techniques used to study these cytoplasmic contractile proteins, because it is not widely recognized how difficult it is to preserve these elements of the cytoplasmic matrix for electron microscopy. The structure of actin filaments is well preserved for electron microscope observation by negative staining with uranyl acetate (Figure 1). In fact, to a resolution of about 3nm the three-dimensional structure of actin filaments determined by computer image processing of electron micrographs of negatively stained specimens (Moore et al., 1970) is indistinguishable from the structure revealed by X-ray diffraction of living muscle.

Sem Studies of Co-Cr-Mo Surgical Implant Alloy Corrosion Behavior

1982 ◽  
Vol 40 ◽  
pp. 520-521
Author(s):  
Ann Chidester Van Orden ◽  
John L. Chidester ◽  
Anna C. Fraker ◽  
Pei Sung
Keyword(s):  
Electron Microscopy ◽  
Corrosion Behavior ◽  
Anodic Polarization ◽  
Saline Solution ◽  
Saturated Calomel Electrode ◽  
Physiological Saline ◽  
X Ray ◽  
Physiological Saline Solution ◽  
Scanning Electron

The influence of small variations in the composition on the corrosion behavior of Co-Cr-Mo alloys has been studied using scanning electron microscopy (SEM), energy dispersive x-ray analysis (EDX), and electrochemical measurements. SEM and EDX data were correlated with data from in vitro corrosion measurements involving repassivation and also potentiostatic anodic polarization measurements. Specimens studied included the four alloys shown in Table 1. Corrosion tests were conducted in Hanks' physiological saline solution which has a pH of 7.4 and was held at a temperature of 37°C. Specimens were mechanically polished to a surface finish with 0.05 µm A1203, then exposed to the solution and anodically polarized at a rate of 0.006 v/min. All voltages were measured vs. the saturated calomel electrode (s.c.e.).. Specimens had breakdown potentials near 0.47V vs. s.c.e.

Sign in / Sign up

Export Citation Format

Share Document