Competitive Exams: Revision Terminology Part 7

  • Fluorescence microscopy – absorb UV & emit visible light. (Flurochromes)

  • Staining technique not used for living cells.

  • Normal skin interference contrast microscopy – for mitosis

  • Polarization microscope – highly ordered structure e.g. spindle fibres

  • In electronic microscope wavelength is much shorter than visible light.

  • High Voltage Electronic microscope – available for TEM – study virus in natural moist condition Resolving power of e microscope = 100 times more than light microscope

  • Janus green – mitochondria

  • Fast green – cytoplasm /cellulose

  • Fuelgen nuclear reaction – acid hydrolysis remove purine at level of purine – dioxyribose glycosidic bond of DNA – unmasking aldehyde group of de-oxyribose, free aldehyde group act as schiff’s reagent

  • Autoradiography technique – path of carbon in photosynthesis.

  • Chromatography by Michel Ts wett (Russian botanist).

  • Study DNA metabolism – tritiated thymine is used.

  • Autoradiography amount of DNA, RAN & protein known at a time

  • Rennet tablets from engineering remain coagulate milk protein – casein

  • Enzyme – prosthetic group = cofactor /coenzyme vitamins enzyme – pH = 6.0-7.5

  • Pepsin – pH =2.0

  • Trypsin – pH = 8.8

  • Enzymes are thermo labile – So dry seeds can endure higher temp then germinating seeds.

  • Enzyme in living cell in inactive form = Zymogen/proenzyme

  • Pepsinogen Stomach(H+) pepsin

  • Self-catalysis = autocatalysis

  • Enterokinase: trypsinogen enterokinase Trypsin

  • Lactice acid dehydrogenase (LDH) = 5 isoenzymes.

  • Number of active sites of enzyme affect turnover number

  • 3D shape of molecule –

    (1) Spatial sit – tertiary structure Match shape of groove

    (2) Bonding fit – present of active site in grooves

  • Induced fit theory – Koshland (enzyme e active site are more flexible)

  • Lock & key theory – Fischer

  • Change in arrangement of polypeptide chain within protein = Denaturation

  • Michaels constant km => Vmax2

  • Initial velocity V0 = Vmax(s)km+(s)

  • Carbonic anhydrase = fastest acting enzyme (low Ki, low enzyme inhibition so more active)

  • Prosthetic group + apoenzyme = Holoenzyme

    (non-protein) (Protein)

  • Enzyme bromeclaim = pineapple

  • Catalytic efficiency = K cat (turnover no.)/Km.(michalies const)

  • Evolve O2 from tissue = peroxidase

  • Histidine decarboxylase = lyase (split) -> fumarase, Aldolase

  • Sulpha drug inhibit synthesis of folic acid in bacteria

  • Cyanide kill organism by inhibiting Cytochrome oxidase

  • Thomas tech – group I r RNA of tetrahymena thermophile could splice itself without help of any protein i.e. RNA can act as Catalyst (enzyme). 1982

  • 1983 – Sydney altman & Norman pace – M/RNA port alone of E coli RNAase enzyme is sufficient for Catalysis, protein is needed for stabilization

  • 1992 – Harry Noller – protein synthesis formation of peptide bond is catalyzed by 235 r RNA & not by protein peptidyl transferase

  • Calvin Melwin – in cyclotron strongly irritated CO2 & H2 end products were HCOOH, Succinic acid & Oxalic acid

  • Presence of abundant free O2 on earth today is not conductive to origin of life.

  • Coacervates - due to Zwitterionic nature, proteins formed colloidal hydrophilic Complexes

  • Homologous organ – Same origin & difference function – forelimbs of vertebrates, leg in insects, teeth of man, thorn of Bougainvillea & tendril of possiflora

  • Analogous organ - difference origin but same function – wing of bird, lead of plant & cladode of Ruscus.