A & P Lecture Test 1

Front 1

anatomy

Back 1

structure and relationships of body parts

Front 2

physiology

Back 2

study of body functions-dynamic system. depends on the way the part is constructed

Front 3

gross anatomy

Back 3

study of large body structures visible to the unaided eye

Front 4

systematic anatomy

Back 4

organized by function

Front 5

surface anatomy

Back 5

study of features that can be observed or touched (palpated)

Front 6

microscopic anatomy

Back 6

study of small structures that require a microscope

Front 7

cytology

Back 7

study of cells

Front 8

histology

Back 8

study of tissues

Front 9

radiography

Back 9

production of images of internal body structures using x-rays

Front 10

angiography

Back 10

use of radiopaque substance to examine arteries of heart or brain (like x- ray)

Front 11

tomography

Back 11

producing sectional images of the body - seperates soft from dense CT CAT scan

Front 12

PET

Back 12

positron emission tomography- isotopes are combined with molecules to view activity of the part ( brain scan)

Front 13

MRI

Back 13

magnetic resonance imaging - magnetic field causes certain atoms to emit weak radio waves which generates a cross sectional image

Front 14

medical terminology?

Back 14

to discuss without long explanations ( latinized & prefixes suffixes)

Front 15

variation

Back 15

normal within set limits. (body temp) normal = average

Front 16

homeostasis

Back 16

body's internal enviroment strives to remain certain limits

Front 17

negative feedback

Back 17

causes variable to change in a direction opposite of the initial change returning it to ideal value

Front 18

positive feedback

Back 18

causes variable to change in the same direction as initial change causing variable to deviate farther from ideal value

Front 19

level of organization in body

Back 19

organ systems, organs, tissues, cells, organelles, molecules, atoms

Front 20

landmarks

Back 20

axillae- armpit
antebrachial fossa- inner elbow

Front 21

quadrants

Back 21

divide abdominal into 4 sections (RUQ, LLQ)

Front 22

regions

Back 22

abdominal/ pelvic region divided into 9 - (umbillical, lumber, hypochondriac, iliac, hypogastric)

Front 23

anatomical position

Back 23

standing in front of you, erect, palms up

Front 24

posterior cavaties

Back 24

cranial (head)
vertbral (spinal cord)

Front 25

anterior cavaties

Back 25

thoracic, diaphragm, abdominal/pelvic

Front 26

visceral organs

Back 26

organs within a body cavity

Front 27

pleural
pericardial
abdominalpelvic/peritonal

Back 27

lungs
heart
guts & abdominal cavity

Front 28

visceral serosa
parietal serosa
serous fluid

Back 28

closer to organ
outer layer
potential space to reduce friction

Front 29

potential energy
kinetic energy

Back 29

stored; capability to do work
in motion / action

Front 30

chemical energy
radiant energy
electrical energy

Back 30

stored in bonds of chem. substances

light- xrays- heat

flow of electrons or other charged particles

Front 31

elements

Back 31

cannot be split into smaller substances by chemical reaction ( O, C, H, N, Ca)

Front 32

atoms

Back 32

smalles unit that can enter a chem. reaction

Front 33

molecule

Back 33

2 or more atoms combined

Front 34

compound

Back 34

can be broken into 2 or more elements

Front 35

exergonic bond

Back 35

bond broken has more energy than one being formed

Front 36

endergonic bond

Back 36

requires energy

Front 37

electron shell

Back 37

holds specific # of electrons- outer shell tries to hold a given # of electrons

Front 38

valence

Back 38

number of elctrons needed to complete the outer shell

Front 39

ion
electrolytes

Back 39

charged particle
ions that carry an electrical current ( Na, K, Cl)

Front 40

ionic bond

Back 40

opposites attract (NaCl)

Front 41

isotope

Back 41

same atomic number but diff. atomic weight
number= protons
weight = protons and neutrons

Front 42

covalent bonds

Back 42

share electron pairs

Front 43

free radical

Back 43

contains unpaired electrons

Front 44

hydrogen bonds

Back 44

2 other atoms associate with H+ atom..weak but biologically

Front 45

inorganic compounds

Back 45

no carbon atoms- ionize in water(break apart to form individual ions)

Front 46

water ( in inorganic compounds)

Back 46

participate in chem reactions, high heat capacity (no great temp change), solvent & suspending medium (polar covalent bonds allow dissolving action)

Front 47

acid
base
salt

Back 47

one or more H+ ion & anion (-)
one or more OH-ion and cation(+)
cation or anion which are not H+ or OH-

Front 48

pH scale

Back 48

below 7 acid
above 7 base
7 neutral
powers of 10

Front 49

buffers

Back 49

stop changes in pH (changes Strong acid or bases to Weak)

Front 50

Organic compounds

Back 50

Carbon compounds mostly held together by covalent bonds (share electrons)

Front 51

dehydration synthesis

Back 51

2 monomers join, eliminating a molecule of water, forming a polymer

Front 52

Hydrolisis

Back 52

molecule of water breaks polymer into monomers

Front 53

carbohydrates

Back 53

sugars, starches, glycogen,(all major energy) cellulose

Front 54

monosaccharide
disaccharide
polysaccharide

Back 54

3-7 carbon (glucose)
2 monosacchardies (sucrose)
hundreds of monosaccharides ( gycogen, starches, cellulose)

Front 55

lipids

Back 55

fatty acid - long carbon chain with H atoms. ends in carboxylic acid group COOH

Front 56

glycerides

Back 56

glycerol & 1,2,3 fatty acids

Front 57

saturated

polyunsaturated

Back 57

with H+ ions (single bond)

more than one double bond
("bad" fat = red meat, milk, cheese)

Front 58

phospholipids

Back 58

glycerol & 2 fatty acidsplus phospate linked to N containing charged group (cell membrane & mem. structure)

Front 59

steroid

Back 59

nonpolar- fat soluble; unique 4 ring structure (cholesterol is precursor of other steroids)

Front 60

prostaglandin

Back 60

5 carbon ring fatty acid (may cuase pain, inflammation)

Front 61

proteins

Back 61

amino acids combined by peptide bond- dehydration synthesis, contain nitrogen, 100,000 diff. types, 20% weight

Front 62

structural organization of proteins

Back 62

primary - 100's of aa in particular order

secondary- twisting or folding of neighboring aa (alpha helix) pleated sheet

tertiary- 3D shape important to function

quaternary- arrangement of chains

denaturation- loss of shape- nonfunctional

Front 63

functions of proteins

Back 63

building blocks (keratin collagen)
Enzymes- biological catalyst (speeds up reaction without entering into reaction itself)

Front 64

2 parts of protein

Back 64

apoenzyme- protein portion
cofactor-nonprotein portion (iron, zinc)
or
coenzyme- organic molecule as vitamin

work only on specific substrates due to 3D shape

Front 65

protein efficiency

Back 65

reaction 100-1000 times more rapid then without enzyme
-ase suffix

oxidases - add oxygen
ATPases- split ATP (high energy compound of cell)
anhydrases- remove water
proteases- break down protein

Front 66

DNA

Back 66

deoxyribonucleic acid - double helix, nucleotide (phosphate, sugar, nitrogen base)

Front 67

bases - A T C G

Back 67

adenine, thymine, cytosine, guanine A-T C-G

Front 68

RNA

Back 68

uracil replaces thymine

Front 69

gene

Back 69

sequence of DNA coding for a particular thing as a protein - enzyme

Front 70

codon

Back 70

3 bases coding for an amino acid